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PubMed2000

Radiofrequency catheter modification of atrioventricular junction in patients with COPD and medically refractory multifocal atrial tachycardia.

BACKGROUND: Multifocal atrial tachycardia (MAT) is a difficult clinical problem generally associated with acute cardiorespiratory illness. The purpose of this study was to assess the feasibility and clinical usefulness of atrioventricular (AV) junction modification as a nonpharmacologic therapy for medically refractory MAT. METHODS AND RESULTS: Thirteen patients with COPD and medically refractory MAT underwent AV junction modification. Complications and outcome of this procedure were monitored. Subjective perceptions of quality of life assessed by a semiquantitative questionnaire and cardiac performance study were obtained before ablation (baseline) and 1 and 6 months after ablation. Radiofrequency energy was applied until the average ventricular rate fell to < 100 beats/min. Ablation procedures controlled the ventricular response in 11 of 13 patients (84%). One patient had unsuccessful modification. Another patient developed delayed complete AV block on the second day after ablation. In these 13 patients, average ventricular rate was reduced from a mean of 145 +/- 11 to 89 +/- 22 beats/min immediately after the ablation (p < 0.01). One patient had recurrent symptomatic MAT at 1 month after ablation; this patient underwent a second procedure without late recurrence. All patients were followed up for at least 6 months (mean, 11 +/- 5 months; range, 6 to 18 months). General quality of life and frequency of significant symptoms improved significantly in patients with successful modification at 1 and 6 months. The left ventricular ejection fraction increased significantly after ablation (44.5 +/- 7.3% at baseline, 49.4 +/- 4. 2% at 1 month, and 50.0 +/- 4.9% at 6 months; all p < 0.05). However, right ventricular ejection fraction remained unchanged (34.7 +/- 6. 2% at baseline, 35.7 +/- 4.4% at 1 month, and 34.3 +/- 4.6% at 6 months; all p > 0.05). The consumption of health-care resources (including frequency of hospital admission and emergency department attendance, antiarrhythmic drug trials) decreased significantly 6 months after AV junction modification. Pulmonary function and theophylline level remained unchanged during follow-up. CONCLUSIONS: AV junction modification offers an effective therapy for controlling ventricular rate in medically refractory MAT. This procedure improves the quality of life and left ventricular function in selected patients with symptomatic and medically refractory MAT.

Aged↗
PubMed2000

PIP2 and ATP cooperatively prevent cytosolic Ca2+-induced modification of ATP-sensitive K+ channels in rat pancreatic beta-cells.

The factors that influence functional coupling between the sulfonylurea receptor (SUR1) and Kir6.2 subunits of ATP-sensitive K+ (K+(ATP)) channels were studied in rat pancreatic beta-cells using patch clamp and microfluorometric techniques. Tolbutamide at 10 micromol/l inhibited K+(ATP) channels in association with occurrence of action currents, but further exposure of beta-cells to the drug for 30 min or longer resulted in reappearance of K+(ATP) channel events. Half-maximal inhibition concentration (IC50) for tolbutamide was 1.5 microl/mol in 2.8 mmol/l glucose, and it was increased to 13.3 micromol/l when the cellular metabolism was inhibited by 0.5 mmol/l 2,4-dinitrophenol (DNP) for 5 min. Tolbutamide at 10 micromol/l induced an increase in cytosolic Ca2+ concentration ([Ca2+]i), and its amplitude was markedly reduced following exposure to 0.5 mmol/l DNP or long-term (30 min) exposure to 10 micromol/l tolbutamide. This tolbutamide insensitivity, as assessed by the [Ca2+]i response, was not observed when the external Ca2+ was omitted during the long-term exposure to tolbutamide. In cell-attached membrane patches, the tolbutamide insensitivity was also produced by treatment of cells with 150 micromol/l diazoxide and 25 mmol/l KCl in the presence, but not absence, of 2 mmol/l Ca2+ in the external solution. When the cytoplasmic face of inside-out membrane patches was treated with higher Ca2+ concentrations (2 micromol/l), both ADP-evoked activation and tolbutamide-induced inhibition of K+ ATP channels were attenuated with retaining ATP-induced inhibition, indicating the modification of K+(ATP) channels. The Ca2+-induced channel modification was prevented partially by phosphatidylinositol 4,5-bisphosphate (PIP2) and completely by ATP and PIP2 together, but not by ATP alone. Treatment of the channel with cytochalasin D, a disrupter of F-actin, evoked channel modification similar to that induced by Ca2+. The modification was prevented completely by phalloidin, a stabilizer of F-actin. In conclusion, long-term exposure to tolbutamide or metabolic inhibition causes modification of K+ ATP channels via mechanisms involving Ca2+-dependent reaction. The modification, which may reflect functional disconnection between SUR1 and Kir6.2, is prevented by ATP and PIP2, which may act cooperatively to stabilize membrane cytoskeletons (F-actin structures).

2,4-Dinitrophenol↗
PubMed1994

Alpha-A crystallin: quantitation of C-terminal modification during lens aging.

Previous studies have demonstrated that the C-terminal region of alpha-A crystallin is susceptible to age-dependent, posttranslational modification. To quantitate the amount of modification, alpha-A crystallin was purified from total proteins of the aging bovine lens, then digested with lys-C endoproteinase. Reverse phase, high pressure liquid chromatography was used to resolve and quantitate the resulting peptides, to determine the amount of C-terminal peptide relative to peptides from other regions of the protein that have not been reported to undergo modification. The results indicate that relative to alpha-A crystallin from newborn lens, posttranslational modification has occurred in approximately 45-55% of the C-terminal region from mature lens. These results demonstrate extensive modification of the C-terminal region of alpha-A crystallin from the mature lens, indicating that during the aging process, posttranslational modifications in this region may make significant contributions to the aggregated state and/or molecular chaperone properties of the molecule.

Aging↗
PubMed2001

Bacterial modification of LPS and resistance to antimicrobial peptides.

Antimicrobial peptides (APs) are ubiquitous in nature and are thought to kill micro-organisms by affecting membrane integrity. These positively charged peptides interact with negative charges in the LPS of Gram-negative bacteria. A common mechanism of resistance to AP killing is LPS modification. These modifications include fatty acid additions, phosphoethanolamine (PEtN) addition to the core and lipid A regions, 4-amino-4-deoxy-L-arabinose (Ara4N) addition to the core and lipid A regions, acetylation of the O-antigen, and possibly hydroxylation of fatty acids. In Salmonella typhimurium, LPS modifications are induced within host tissues by the two-component regulatory systems PhoPQ and PmrAB. PmrAB activation results in AP resistance by Ara4N addition to lipid A through the activation of at least 8 genes, 7 of which are transcribed as an operon. Loss of this operon and, therefore, Ara4N LPS modification, affects S. typhimurium virulence when administered orally. Transposon mutagenesis of Proteus mirabilis also suggests that LPS modifications affect AP resistance and virulence phenotypes. Therefore, LPS modification in Gram-negative bacteria plays a significant role during infection in resistance to host antimicrobial factors, avoidance of immune system recognition, and maintenance of virulence phenotypes.

Amino Sugars↗
PubMed2002

Mechanical failure of the American Medical Systems Ultrex inflatable penile prosthesis: before and after 1993 structural modification.

PURPOSE: The 700 Ultrex (American Medical Systems, Minnetonka, Minnesota) is the only penile prosthesis capable of length and girth expansion. Early experience with the 700 Ultrex showed an increased mechanical failure rate compared with the 700CX, mostly secondary to cylinder failure. In 1993 the Ultrex cylinders were modified. We examined the performance of the Ultrex device before and after modification. MATERIALS AND METHODS: We compared our results with the Ultrex prosthesis before (group 1) and after (group 2) the 1993 modification. We implanted 239 devices from October 1989 to December 1999. A total of 26 patients have died. Followup was obtained on the results of 137 of the remaining 213 implants (64%), including 85 pre-modification devices in 85 patients and 52 post-modification devices in 51, via a mailed questionnaire, telephone survey or chart review. The questionnaire and survey included a 5-point satisfaction scale. Groups 1 and 2 were compared in regard to 3 end points, namely cylinder, mechanical and overall failure. RESULTS: Followup was less than 1 to 136 months (median 92, 25th to 75th percentiles 43 to 108) in group 1 and less than 1 to 92 months (median 46, 25th to 75th percentiles 21 to 75) in group 2. The 5-year Kaplan-Meier estimates of overall, mechanical and cylinder survival in groups 1 and 2 were 64.7%, 70.7% and 80.2%, and 77.7% (p = 0.23), 93.7% (p = 0.017) and 96.2% (p = 0.008), respectively. Overall satisfaction was similarly high in groups 1 and 2 (mean 3.9 and 4 points). CONCLUSIONS: On long-term followup the 1993 modification of the Ultrex cylinders appears to have significantly decreased the propensity of cylinder failure of the pre-modification device.

Adult↗
PubMedDate not supplied

Simulating smokers' acceptance of modifications in a cessation program.

Recent research has underscored the importance of assessing barriers to smokers' acceptance of cessation programs. This paper illustrates the use of computer simulations to gauge smokers' response to program modifications which may produce barriers to participation. It also highlights methodological issues encountered in conducting this work. Computer simulations were based on conjoint analysis, a consumer research method which enables measurement of smokers' relative preference for various modifications of cessation programs. Results from two studies are presented in this paper. The primary study used a randomly selected sample of 218 adult smokers who participated in a computer-assisted phone interview. Initially, the study assessed smokers' relative utility rating of 30 features of cessation programs. Utility data were used in computer-simulated comparisons of a low-cost, self-help oriented program under development and five other existing programs. A baseline version of the program under development and two modifications (for example, use of a support group with a higher level of cost) were simulated. Both the baseline version and modifications received a favorable response vis-à-vis comparison programs. Modifications requiring higher program costs were, however, associated with moderately reduced levels of favorable consumer response. The second study used a sample of 70 smokers who responded to an expanded set of smoking cessation program features focusing on program packaging. This secondary study incorporate in-person, computer-assisted interviews at a shopping mall, with smokers viewing an artist's mock-up of various program options on display. A similar pattern of responses to simulated program modifications emerged, with monetary cost apparently playing a key role. The significance of conjoint-based computer simulation as a tool in program development or dissemination, salient methodological issues, and implications for further research are discussed.

Adolescent↗
PubMed1990

Chemical modification of chloroperoxidase with diethylpyrocarbonate. Evidence for the presence of an essential histidine residue.

Chloroperoxidase from Caldariomyces fumago is well documented as an extremely versatile catalyst, and studies are currently being conducted to delineate the fine structural features that allow the enzyme to possess chemical and physical similarities to the peroxidases, catalases, and P-450 cytochromes. Earlier investigations of ligand binding to the heme iron of chloroperoxidase, along with the presence of an invariant distal histidine residue in the active site of peroxidases and catalases, have led to the hypothesis that chloroperoxidase also possesses an essential histidine residue that may participate in catalysis. To address this in a more direct fashion, chemical modification studies were initiated with diethylpyrocarbonate. Incubation of chloroperoxidase with this reagent resulted in a time-dependent inactivation of enzyme. Kinetic analysis revealed that the inactivation was due to a simple bimolecular reaction. The rate of inactivation exhibited a pH dependence, indicating that modification of a titratable residue with a pKa value of 6.91 was responsible for inactivation; this data provided strong evidence for histidine derivatization by diethylpyrocarbonate. To further support these results, inactivation due to cysteine, tyrosine, or lysine modification was ruled out. The stoichiometry of histidine modification was estimated by the increase in absorption at 246 nm, and it was found that more than 1 histidine residue was derivatized when chloroperoxidase was inactivated with diethylpyrocarbonate. However, it was shown that the rates of modification and inactivation were not equivalent. This was interpreted to reflect that both essential and nonessential histidine residues were modified by diethylpyrocarbonate. Kinetic analysis indicated that modification of a single essential histidine residue was responsible for inactivation of the enzyme. Studies with [14C]diethylpyrocarbonate provided stoichiometric support that derivatization of a single histidine inactivated chloroperoxidase. Based on sequence homology with cytochrome c peroxidase, histidine 38 was identified as a likely candidate for the distal residue. Molecular modeling, based on secondary structure predictions, allows for the construction of an active site peptide, and implicates a number of other residues that may participate in catalysis.

Amino Acid Sequence↗
PubMed1987

[Phenotypic characteristics of a new modification-restriction system in E. coli].

It has been demonstrated phenotypically that there exists a new modificational-and-restrictional system as synthesized by the recombinant Escherichia coli tF strain. A series of passages of the T3 and T7 phages and their mutants in E. coli tF has made it possible to ascertain a specific modification of the phage DNA, with was shown to be induced by the host strain. The high level of adsorption of these phages on the cell surface of E. coli tF has ruled out the possibility of existing of a 'nonclassical' modification and restriction of DNA. In view of the further characterizing of this modificational-and-restrictional system of E. coli tF it has been comparatively studied with the already known modificational-and-restrictional systems isolated from various Escherichia coli strains. Results have shown that no identity exists between the tested systems and the one in E. coli tF. It is stated that the new modificational-and-restrictional system of E. coli tF belongs to none of the three known types of restrictional endonucleases.

Adsorption↗
PubMed1986

Chemical modification of thiol groups of mitochondrial F1-ATPase from the yeast Schizosaccharomyces pombe. Involvement of alpha- and gamma-subunits in the enzyme activity.

Mitochondrial F1-ATPase from the yeast Schizosaccharomyces pombe has been prepared under a stable form and in relatively high amounts by an improved purification procedure. Specific chemical modification of the enzyme by the thiol reagent N-ethylmaleimide (NEM) at pH 6.8 leads to complete inactivation characterized by complex kinetics and pH dependence, indicating that several thiols are related to the enzyme activity. A complete protection against NEM effect is afforded by low concentrations of nucleotides in the presence of Mg2+, with ADP and ATP being more efficient than GTP. A total binding of 5 mol of [14C]NEM/mol of F1-ATPase is obtained when the enzyme is 85% inactivated: 3 mol of the label are located on the alpha-subunits and 2 on the gamma-subunit. Two out of the 3 mol on the alpha-subunits bind very rapidly before any inactivation occurs, indicating that the two thiols modified are unrelated to the inactivation process. Complete protection by ATP against inactivation by NEM prevents the modification of three essential thiols out of the group of five thiols labeled in the absence of ATP: one is located on a alpha-subunit and two on the gamma-subunit. These two essential thiols of the gamma-subunit can be differentiated by modification with 6,6'-dithiodinicotinic acid (CPDS), another specific thiol reagent. A maximal binding of 4 mol of [14C]CPDS/mol of enzyme is obtained, concomitant to a 25% inhibition. Sequential modification of the enzyme by CPDS and [14C]NEM leads to the same final deep inactivation as that obtained with [14C]NEM alone. One out of the two thiols of the gamma-subunit is no longer accessible to [14C]NEM after CPDS treatment. When incubated at pH 6.8 with [3H]ATP in the presence of Mg2+, F1-ATPase is able to bind 3, largely exchangeable, mol of nucleotide/mol of enzyme. Modification of the three essential thiols by NEM dramatically decreases the binding of 3H-nucleotide down to about 1 mol/mol of enzyme. Partial modification modifies the cooperative properties, the enzyme being no longer sensitive to anion activation.

Adenosine Triphosphate↗
PubMed1978

[Chemical modification of epsilon-amino lysine groups in horseradish peroxidase. Its effect on catalytic properties and spatial structure of the enzyme].

Effect of chemical modification of horseradish peroxidase lysine epsilon-amino groups by propionic, butyric, valeric, succinic anhydrides and trinitrobenzolsulfonic acid (TNBS) on catalytic properties of the enzyme is investigated. All the preparations of modified peroxidase have 100% peroxidase activity for o-dianizidine at pH 7.0, which indicates the absence of lysine epsilon-amino group in the enzyme active site. pH-dependencies of modified peroxidase relative activity are studied; modification by anhydrides of monobasic acids is not found to result in changes of the relative activity pH-profile, while modification by succinic anhydride widens it. Absorption and circular dichoism spectra of native and modified peroxidase within 260--270 nm are obtained, some changes in the enzyme tertiary structure after its epsilon-amino groups modification are observed. Modification of four epsilon-amino groups by buturic and succinic anhydrides and of three epsilon-amino groups by TNBS is found to increase the regidity of protein surrounding of heme, and modification of six epsilon-amino groups by TNBS results in more unwrapped enzyme structure as compared with its native molecule.

Butyrates↗
PubMed1987

Protein damage and degradation by oxygen radicals. II. Modification of amino acids.

Exposure of proteins to the hydroxyl radical (.OH) or to the combination of .OH plus the superoxide anion radical (.OH + O2-) causes gross structural modification. Such modified proteins can undergo spontaneous fragmentation or can exhibit substantial increases in proteolytic susceptibility. In the present study, with the representative protein bovine serum albumin (BSA), we report that alterations to primary structure underlie such gross structural modifications. All amino acids in BSA were susceptible to modification by both .OH and .OH + O2- +O2), although tryptophan, tyrosine, histidine, and cysteine were particularly sensitive. At a radical/BSA molar ratio (nmol of radicals/nmol of BSA) of 10, we observed an average 9-10% destruction of amino acids; whereas at a ratio of 100, the average loss was 45%. Decreasing tryptophan fluorescence provided a useful index of amino acid loss and exhibited a clear dose dependence with .OH or with .OH + O2- (+O2). Linear production of the biphenol bityrosine was observed with .OH treatment. In contrast, .OH + O2- (+O2) induced only a limited bityrosine production rate which reached an early plateau. Studies with various chemical scavengers (t-butyl alcohol, isopropyl alcohol, mannitol, urate) and gasses (N2O, N2, O2, air) revealed that .OH is the primary radical responsible for all amino acid modifications, but that O2- and O2 can further transform the products of .OH reactions. Thus, O2-/O2 can potentiate .OH-dependent destruction of many amino acids (e.g. tryptophan) while inhibiting production of bityrosine by reacting with tyrosyl (phenoxyl) radicals. No amino acid loss or bityrosine production occurred with exposure to O2- (+O2) alone. Amino acid modifications caused both by .OH alone and by .OH + O2- (+O2) progressively affected the overall electrical charge of BSA. In a pH range of 3.7-6.2, some 16 new isoelectric focusing bands were induced by .OH, and some eight new bands were induced by .OH + O2- (+O2). The alterations to primary structure observed provide the key to an understanding of the link between oxidative modification and increased proteolytic susceptibility.

Amino Acids↗
PubMed1986

[Activation of oncogenes by chemical modification with carcinogens].

This article reviews the chemical modification of DNA (mainly proto-Ha-ras sequence) which causes mutation and induction of transforming activity. An initial chemical event caused by chemical carcinogens is modification of DNA with metabolically activated carcinogens. The chemical modification of DNA is thought to result in activation of oncogenes by mutation or reconstruction. The activated transforming oncogenes (mainly of the ras family, by point mutation) have been found in tumors induced by diverse carcinogens in vivo (reviewed briefly). Recently, results establishing that chemical modification of proto-oncogenes with carcinogens, such as benz (a) pyrene, acetylaminofluorene, Glu-P-1, 4NQO, and aflatoxin B1, induces transforming activity of the gene when transfected into NIH3T3 cells have been reported. The mechanism of activation of proto-Ha-ras by chemical modification has been investigated by RFLP (restriction fragment length polymorphism) assay and/or Southern blot analysis using synthetic oligonucleotides. Point mutations at codon 12 or 61 have been found. The correlation between the established chemistry of chemical modification of DNA with diverse carcinogens and activation of proto-oncogenes is discussed.

9,10-Dimethyl-1,2-benzanthracene↗
PubMed1987

Postsynthetic modification of human enolase isoenzymes.

The original form of beta beta enolase (EC 4.2.1.11) in tissue is modified to two more electrophoretically distinct forms when incubated with human serum. The three postsynthetic forms are designated beta beta 3, beta beta 2, and beta beta 1, in order of increasing anodal mobility and increasing modification. Serum and carboxypeptidases A and B all produce identical modifications of beta beta enolase but exhibit very different pH-activity profiles. A purified human serum protein previously named "modifying protein," which is responsible for the modification of creatine kinase-M and alpha-enolase subunits, modifies beta beta enolase and also has a pH-activity profile identical to that for serum. Thus we conclude that the modifying protein is not identical to either carboxypeptidase A or B; it may, however, be an as-yet-undescribed carboxypeptidase. With increased modification, both alpha alpha and beta beta enolase decrease in apparent activation energy; gamma gamma enolase shows no evidence of modification, and its apparent activation energy remains stable. Measurement of activation energy is an easy tool for screening for postsynthetic modifications in an enzyme.

Carboxypeptidase B↗
PubMedDate not supplied

[Modification of the RNA-polymerase of Escherichia coli by diethylpyrocarbonate].

E. coli DNA dependent RNA polymerase was modified by diethylpyrocarbonate. Optical and kinetic properties of the reaction were studied. More than 90% of RNA polymerase activity is inhibited by introduction of 9--11 ethoxyformyl groups per enzyme molecule without loss of its ability to bind DNA template. Furthermore the modified enzyme is able to form tight complexes with DNA and to compete with native enzyme for the formation of rifampicin-resistant complex. The ratio of the complex formation constants for the native and modified enzyme was determined to be equal to 10. The enzyme modified to such extent loses the activity in DNA dependent RNA as well as pppApU synthesis. Vmax value rather than Km value for both ATP and UTP decreases following the modification reaction. Incubation of the enzyme modified to the 10% of residual activity with 0.2 M hydroxylamine for 2 hours results in restoration of RNA polymerase activity. Most but not all of the modified histidyl residues restore their native structure. Two of 13 histidyl residues were modified irreversibly due to Bamberger's cleavage reaction, but these two residues were found to be unessential for RNA polymerase activity. Reaction with higher concentration of the diethylpyrocarbonate induces modification of more than 15--20 histidyl residues and leads to irreversible inactivation of the enzyme. Nevertheless the modification of the additional histidyl redidues was reversible as well as the modification of the first 11 residues. RNA polymerase modified to such extent loses the ability to bind DNA. Preformation of the initiated ternary complex of RNA polymerase with template and product fails to protect the enzyme from reversible inactivation at a low reagent concentration, but markedly decreases the rate of the irreversible and unspecific modification of sulfhydryl or amino groups of the enzyme. Reaction with the ternary complex results in reversible inactivation of the enzyme with respect to elongation of RNA chains as well as the pyrophosphate exchange reaction. The complex itself was, however, completely stable under the reaction conditions and the enzyme subunit structure was also conserved after the reaction. Evidently, the mild modification of the histidyl residues with diethylpyrocarbonate selectively inhibits RNA chain elongation.

Chemical Phenomena↗
PubMedDate not supplied

Reflex modification as a test for sensory function.

Reflex modification is a versatile procedure for the assessment of sensory function because it can provide information about the responses of several sensory systems to both weak and intense stimuli. The procedure has two elements: The elicitation of some reflex, such as the acoustic startle reflex, and the modification of that reflex by preliminary stimuli. In these experiments we used reflex modification and reflex elicitation procedures to examine the normal development of auditory function in rats and to evaluate alterations in auditory function produced by physical and toxic insult. Adult rats exposed to octave bands of noise demonstrated frequency-specific deficits on a test of reflex modification, but not reflex elicitation. In the studies of developing rats, reflex elicitation appeared by postnatal day 12 and modification around day 14. Frequency-specific increases in both measures suggested that the phenomena were sensitive to auditory development and, not simply, motor development. Exposure to kanamycin on postnatal days 8 to 16 produced dose-related deficits in the ability to detect stimuli at 32 and 16 kHz, but not 4 and 0.8 kHz. These effects were observed in the absence of changes in reflex elicitation. The results demonstrate that reflex modification procedures provide more sensitive and specific information than that provided by the use of reflex elicitation alone.

Acoustic Stimulation↗
PubMed1986

Treatment of fecal incontinence in children with spina bifida: comparison of biofeedback and behavior modification.

Two experiments compared the effects of biofeedback training to behavior modification in the treatment of 33 children aged 5 to 16 who had fecal incontinence secondary to myelomeningocele. Biofeedback involved providing visual feedback and rewards for successively stronger sphincter contractions during training sessions and requiring 50 sphincter contraction exercises daily. Behavior modification involved attempting to defecate immediately after the evening meal each day, receiving a reward for defecating in the toilet without an enema or suppository, and receiving an enema if unsuccessful for two consecutive days. In experiment I, eight children were offered biofeedback alone in an attempt to replicate previous studies. Biofeedback alone was found insufficient; addition of behavior modification was necessary. Experiment II systematically investigated the relative contribution of these two treatments. Overall, patients who received only behavior modification for three months showed as much clinical improvement as patients who received behavior modification plus biofeedback. This suggests that previous reports, because they have not controlled for nonspecific treatment effects, have overestimated the value of biofeedback in this population. However, a subgroup of patients (27%) were identified for whom biofeedback provided additional, specific benefit. These were children who had spinal cord lesions below L-2 and who initially had two or more bowel movements daily. The combination of behavior modification and biofeedback resulted in a greater than 50% reduction in the frequency of incontinence for 64% of patients, and results were well maintained at follow-up one year later.

Adolescent↗
PubMedDate not supplied

[Analysis of parameters for the equation of isotherms of chemical modification for the alkylation of nucleic acids in complexes with chloroethylmethylaminobenzylidene oligonucleotides].

The coincidence between the adsorbtion isotherm E + X in equilibrium or formed from EX (association constant KX) and isotherm of the chemical modification (the dependence of the limit extent of modification r infinity biopolymer E with excess of the reagent X) calculated earlier. Schemes (1) and (2) are given. It was shown that r infinity is identical to [EX]0/e), if (1) and (2-2) are absent due to equality of the rate constants of the conversion of X in complex and in solution, i.e. the isotherm of modification may imitate the adsorbtion isotherm. The influence of the equilibrium (2) at the initial part of the isotherm of modification is not essential, if process (1-1) is absent and y2 = k -P/k1 is small (smaller than or equal to 0.1) and y1 = (k1/k2)(kP/k-PKX) has various magnitudes within y1 x y2 smaller than or equal to 0.1. Once the parameter y1 is equal to unity, the difference between the isotherms of adsorbtion and of modification are small at the initial part in spite of equilibrium (1-1). These results indicate the KX may be calculated from the modification data given earlier in the found range of values of parameters y1 and y2, if e0 is determined by an independent way.

Adsorption↗
PubMed1981

[Phenylalanyl-tRNA synthetase from E. coli MRE-600. Effect of chemical modification of lysine residues on the enzyme interaction with substrates].

The effect of modification of Phe-RSase from E. coli MRE-600 by pyridoxal-5'-phosphate and 2', 3'-dialdehyde derivative of ATP and L-phenylalanynyl-5'-adenylate obtained by periodate oxidation on the enzyme interaction with substrates was investigated. It was shown that modification of Phe-RSase by pyridoxal-5'-phosphate and 2', 3'-dialdehyde derivative of ATP leads to a decrease of the aminoacylation rate without changing the rate of the ATP-[32P]-pyrophosphate exchange reaction. The substrate analogs L-phenylalanynol and L-phenyl-alanynyladenylate increase the degree of Phe-RSase inactivation in the aminoacylation reaction. tRNAphe strongly protects the enzyme against inactivation. ATP, both in the absence (in case of modification with pyridoxal-5'-phosphate) and in- the presence of Mg2+ and phenylalanine (in case of modification with o-ATP) exhibits a pronounced protective effect. L-Phe does not protect the enzyme against the inactivation by pyridoxal-5'-phosphate or o-ATP. The dissociation constant of the Phe-RSase[14C]-Phe-tRNAphe complex increases 2.5 -- 5-fold after the enzyme modification by pyridoxal-5'-phosphate, while the Km value for tRNAphe decreases approximately two times in the aminoacylation reaction. There are no changes in the Km values for amino acid and ATP and the Hill coefficients for all substrates tested. Modification of Phe-RSase by pyridoxal-5'-phosphate leads to a decrease of stability of the aminoacyladenylate -- enzyme complex. Oxidized L-phenylalanynyladenylate does not produce enzyme inactivation either by aminoacylation or in the isotropic ATP-PP iota exchange reaction. It is assumed that Phe-RSase from E. coli MRE-600 contains some lysine residues essential for binding and aminoacylation of tRNA, which do not occur in the ATP-binding subsite and aminoacyladenylate formation center.

Adenosine Triphosphate↗