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PubMed1995

[Stellate ganglion block with transcutaneous electric nerve stimulation (TENS): a double-blind study with healthy probands].

OBJECTIVE: Blockade of the stellate ganglion is an established and highly effective diagnostic and therapeutic procedure for management of certain acute and chronic pain syndromes or other disorders. The paratracheal injection of a local anaesthetic is the simplest and most frequently used approach for blocking the cervicothoracic sympathetic nerves (ganglion stellate). However, since serious complications can occur during or following the anterior paratracheal technique including accidental intravenous or intraarterial injection, non-invasive methods for blockade of the stellate ganglion have been suggested. In 1980 Jenkner (15) reported the successful interruption of the sympathetic outflow from the stellate ganglion together with the relief of pain by transcutaneous electrical nerve stimulation (TENS), followed by the development of an "optimal wave form" in 1981 (14). Since we were unable to reproduce Jenkner's results of sympathetic blockade in our patients, this study was designed to investigate the effects of TENS on the sympathetic activity of the stellate ganglion in healthy volunteers. METHODS: 50 healthy volunteers were randomised into two groups (n = 25). In group I the left stellate ganglion was stimulated for 20 min by the mode described by Jenkner (monophasic pulse, small anode, large cathode, frequency 20 Hz), while group II was stimulated by conventional TENS (biphasic pulse, electrodes of identical size, frequency 100 Hz). The method of stimulation was blinded to both the investigator and the subjects investigated. Measurements included cutaneous blood flow of the volar forearm (laser Doppler), skin temperature on two sites of the cheeks (thermistor), pupil diameter and size of the palpebral fissures, sweat production (ninhydrine test) and global sensitivity and pain perception thresholds on both sides (electrical stimulation). Measurements were performed before TENS of the stellate ganglion, after 5, 10, 15 and 20 min of stimulation and 10 min after termination of TENS. Statistical analysis of the obtained data was performed by Friedman-Test and by Mann-Whitney-U-Test. p < 0.05 was assigned statistical significance. MAIN RESULTS: Skin temperature increased in both groups and on both sides by 1.2 degrees C, while skin perfusion rate, pupil size, size of the palpebral fissure and sweat production remained unchanged. Global sensitivity and pain perception thresholds of forehead decreased in both groups and on both sides, while there was no change of both parameters on the hands. CONCLUSION: No signs and symptoms of sympathetic blockade could be demonstrated in any of the groups, neither by TENS of the stellate ganglion as described by Jenkner nor by unspecific TENS. Thus, pain relief by TENS of the stellate ganglion as reported in the literature must involve other mechanisms than sympathetic blockade. In addition, TENS may not replace traditional blockade of the stellate ganglion by local anesthetics, if sympathetic blockade is required for diagnostic and therapeutic purposes.

Adult↗
PubMed1990

Decreased collagen concentration in rat uterine implantation sites compared with non-implantation tissue at days 6-11 of pregnancy.

Collagen concentrations at implantation sites in the rat uterus were found to be significantly decreased compared with concentrations in adjacent non-involved uterine tissue in early pregnancy (75% by Day 11). The decrease in collagen was most marked in primary decidua and was also observed to a lesser extent (20%) in myometrium at the implantation site. There was a decrease of 20% in the concentration of total proteins at Day 7 (as measured by the ninhydrin method) and a slight increase in water content (2%) at Days 6 and 7. The differences in total protein and water content were transient, but the difference in collagen was maintained throughout early pregnancy. The localized changes in collagen content observed in this study, along with previously reported morphological changes in fibrillar and basement-membrane collagens in the uterus, give support to a theory of remodelling in early pregnancy involving simultaneous synthesis and degradation of extracellular proteins during decidualization.

Animals↗
PubMed1977

Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24.

Chromosomal protein A24 has a unique structure inasmuch as it contains histone 2A and a nonhistone polypeptide the sequence of which has been partially determined. Comparative analysis of the ninhydrin-insensitive amino-terminal tryptic peptides of protein A24 and histone 2A and a quantitative analysis of their carboxyl-terminal amino acid indicated that protein A24 has two amino termini and one carboxyl terminus. The amino acid sequence analysis of tryptic peptide 17' of protein A24: (see text) showed it contains tryptic peptide 17 of histone 2A, Lys-Thr-Glu-Ser-His-His-Lys. Lysine 119, the amino terminus of this peptide, which is derived from the histone 2A portion of protein A24, is linked by an isopeptide bond to the carboxyl group of a glycine residue. Accordingly, the branched structure of protein A24 proposed is: (see text).

Amino Acid Sequence↗
PubMed1978

Isolation of an avian erythrocyte protein possessing ADP-ribosyltransferase activity and capable of activating adenylate cyclase.

An ADP-ribosyltransferase was purified approximately 500-fold from the supernatant fraction of turkey erythrocytes. The enzyme hydrolyzed [carbonyl-(14)C]NAD to ADP-ribose and [carbonyl-(14)C]nicotinamide at a low rate. Nicotinamide formation from NAD was enhanced by arginine methyl ester > D-arginine approximately L-arginine > guanidine; lysine, histidine, and citrulline were ineffective. Incubation of [adenine-U-(14)C]NAD and arginine methyl ester or arginine with the purified enzyme resulted in the formation of new compounds that contained (14)C, reacted with ninhydrin, and quenched background fluorescence of thin-layer plates viewed in ultraviolet light. Their mobilities on thin-layer chromatograms were indistinguishable from those of ADP-ribosylarginine methyl ester and ADP-ribosylarginine formed during incubation of choleragen with NAD and arginine methyl ester or arginine, respectively [Moss, J. & Vaughan, M. (1977) J. Biol. Chem. 252, 2455-2457]. The purified transferase also catalyzed the incorporation of label from [adenine-(14)C]-NAD into lysozyme, histones and polyarginine. When the (14)C-labeled lysozyme was incubated with snake venom phosphodiesterase, the radioactivity was released and, on thin-layer chromatograms, exhibited a mobility indistinguishable from that of 5'-AMP, as would be expected of an ADP-ribosylated protein, but not of a poly(ADP-ribosylated) product. The purified transferase activated rat brain adenylate cyclase and, as is the case with choleragen, activation was absolutely dependent on NAD. The presence in the avian erythrocyte of a protein that, like choleragen and Escherichia coli heat-labile enterotoxin, apparently activates adenylate cyclase and possesses ADP-ribosyl transferase activity is consistent with the view that the mechanisms through which the bacterial toxins produce pathology are not entirely foreign to vertebrate cells, at least some of which may possess and employ an analogous mechanism for activation of adenylate cyclase.

Adenosine Diphosphate Sugars↗
PubMed1979

Degradation of abnormal proteins in intact mouse reticulocytes: accumulation of intermediates in the presence of bestatin.

Incubation of intact mouse reticulocytes with bestatin (a competitive inhibitor of aminopeptidases) produced the accumulation of low molecular weight intermediates in the degradation of puromycinyl-peptides or analog-containing proteins that had been pulse labeled with L-[1-14C]leucine. A large fraction of the radioactive protein was degraded to trichloroacetic acid-soluble products within 10 min. In the presence of bestatin (0.5 mg/ml), one-fourth of these products appeared to be dipeptides, tripeptides, or both: they were resistant to ninhydrin at acid pH (a treatment that decarboxylates only free amino acids) except after intensive acid hydrolysis, and they eluted from a Sephadex G-10 column with an apparent average size of 300 daltons. These radioactive products did not appear if incorporation of the tracer was prevented by prior treatment with cycloheximide, demonstrating that they originated from polypeptide precursors. Thus, a peptidase inhibitor has been successfully used in the production of low molecular weight intermediates in the in vivo degradation of cellular proteins.

Aminopeptidases↗
PubMed1982

Evidence that a reducible xylosyl-lysine is the protein linkage of dermatan sulfate.

Dermatan sulfate, purified by standard methods, displayed one spot at the position of the standard after two-dimensional cellulose acetate electrophoresis and was 99% in GalN, 21.5% in sulfate, and 0.6% in protein; Gal and Xyl (2:1) were the only neutral sugars detected. Its glucuronic acid/iduronic acid ratio was 0.15 and its Mr was approximately equal to 16,000. On reaction with 0.4 M NaOH, its reducing group(s) determined as Glc increased by 71% with concomitant separation of protein and polysaccharide and no alteration of the amino acids; when this reaction was repeated in the presence of 0.3 M NaBH4, only 31% of Lys was detected by standard amino acid analysis and none by TLC of the dansylated amino acids; alkaline cleavage in these conditions yielded only 30% of the original Xyl, xylitol, and a ninhydrin-positive substance different from GalN, which had the retention time of xylitol on Affi-Gel 601 and was also obtained from reduction of dermatan sulfate with a 400-eq excess of Na3BH4 in water under conditions that did not cleave the dermatan sulfate-protein bond. The data indicate that a reducible xylosyl-lysine is the protein linkage of dermatan sulfate from calf ligamentum nuchae.

Amino Acids↗
PubMed1977

Purification and characterization of a cardioexcitatory neuropeptide from the central ganglia of a bivalve mollusc.

We have purified a cardioexcitatory substance, previously designated peak C, from ganglia of the Sunray Venus clam, Macrocallista nimbosa. Low concentrations (10(-9)-10(-8) M) of this substance not only excite the isolated clam heart, but also produce tonic contractions of the isolated radula protractor muscle of the whelk, Busycon contrarium. These two muscle preparations have therefore been used as a parallel bioassay for peak C. Peak C is inactivated by proteolytic enzymes, has an isoelectric point greater than pH 10 and has an ultraviolet absorption spectrum similar to that of phenylalanine. On thin layer chromatograms, peak C separates into two components; one of these is probably a partially oxidized form produced during purification. Both components react with ninhydrin and with the Sakaguchi reagent for guanidino groups. The amino acid composition of peak C is Phe2.00Met0.81Arg1.12. N-terminal analysis, one round of Edman-dansyl degradation, and tryptic digesting are consistent with the identification of Macrocallista peak C as a tetrapeptide amide: Phe-Met-Arg-Phe-NH2 (FMRFamide).

Amino Acid Sequence↗
PubMed1996

Conditions altering plasma concentrations of urea cycle and other amino acids in elderly human subjects.

OBJECTIVE: Describe plasma amino acid concentrations and total urinary amino acid excretion in subjects from an elderly female population. SUBJECTS: Fasting plasma samples, complete 24-hour urine samples, and 3-day diet records were obtained from 96 healthy postmenopausal women in one study and fasting plasma samples were obtained from an additional 44 subjects in 3 separate studies. In one study, nonfasting plasma samples were also collected. The subjects ranged in age from 49 to 80 years of age. Samples were obtained to allow the evaluation of the effects of fasting vs. nonfasting, normal vs. Alzheimers subjects, and level of protein intake effects. MEASURES OF OUTCOME: Heparinized plasma samples were deproteinized with a 5-sulfosalicylic acid solution and centrifuged at 14,900 x g. Deproteinized plasma and urine samples were analyzed for free amino acids on a Beckman System 6300 analyzer using a postcolumn reaction with ninhydrin to quantitate the amino acids. RESULTS AND CONCLUSIONS: It is concluded that: 1) From fasting plasma samples, 1 or 2 sampling days are sufficient to establish a characteristic concentration for most plasma amino acids. 2) Fasting amino acid concentrations do not reflect levels of dietary protein intake when dietary amino acid composition is similar. Shifts in fasting amino acid concentrations would be more indicative of changes in relative amounts of amino acids absorbed rather than level of dietary protein per se. 3) Totals of fasting plasma concentrations of arginine, citrulline and ornithine were relatively constant, but fluctuations occurred in the ratio of ornithine to arginine in the different populations; and 4) Patients with Alzheimers disease exhibited altered plasma ornithine and arginine concentrations relative to active or sedentary controls.

Aged↗
PubMed1991

Chemical synthesis, initial conformational studies, and activity of rat steroidogenesis activator peptide and a truncated analog.

A 30-residue peptide corresponding to the amino acid sequence of steroidogenesis activator peptide (SAP) from rat Leydig tumor cells has been synthesized by the solid-phase method using Boc protection. SAP is the putative cycloheximide-sensitive, cAMP-regulated mediator of ACTH-stimulated conversion of cholesterol to pregnenolone in adrenal cortex. N alpha-acetyl-SAP(11-30), an NH2-terminally truncated steroidogenesis activator peptide analog that is missing the most hydrophobic portion of SAP, was also prepared. In addition to these two peptides, N alpha-acetyl-(Cys0)SAP was synthesized in both non-radiolabeled and tritiated forms for coupling to carrier proteins for use as an immunogen to raise anti-SAP antibodies. Chain elongation during synthesis of SAP on PAM resin proceeded with an average coupling yield of 99.3% as determined by quantitative ninhydrin tests. After HF cleavage at -7 degrees, the crude products were purified by semi-preparative HPLC. Peptides were analyzed by analytical HPLC, amino acid analysis, tryptic peptide mapping, and by UV and CD spectroscopy. As determined by CD spectra, SAP showed little evidence of preferred structure either in aqueous solution in the presence of divalent cations or in micelles of reduced Triton X-100 in the absence or presence of either cholesterol or phosphatidylcholine. SAP, in conjunction with GTP, enhanced side chain cleavage activity in isolated adrenal mitochondria.

Adrenal Glands↗
PubMed2004

A glycosylated byssal precursor protein from the green mussel Perna viridis with modified dopa side-chains.

Foot tissue of the green mussel Perna viridis contains a variety of byssal precursor proteins with the unusual redox-active amino acid, Dopa (-beta-3,4-dihydroxyphenyl-alpha-alanine). Eight proteins were detectable in acidic extracts of the Perna foot by a redox cycling assay with nitroblue tetrazolium. In one of these, however, P. viridis foot protein-1 (Pvfp-1), activity was not due to Dopa, but to another redox-active derivative. Based on specific colorimetric derivatization with Arnow's reagent, ninhydrin and phenylisothiocyanate (Edman), mass spectrometry, the redox-active derivative in Pvfp-1 is not consistent with any known modification. Another uncommon modification of Pvfp-1 involves O-glycosylation of threonine by mannose, glucose or fucose. As in previously characterized fp-1s, the primary sequence of the Pvfp-1 (apparent mass 89 kDa) has two consensus decapeptide motifs; one is APPKPX1TAX2K and the other is APPPAX1TAX2K, where P is Pro/Hyp, and X1 and X2 are difucosylated threonine and a redox sensitive derivative of tyrosine or Dopa, respectively. Of these two unusual residues, X2 is unique to Pvfp-1, whereas O-glycosylated Thr has been previously detected in freshwater mussel fp-1. The sequence homology of Pvfp-1 with the common structural motifs of the fp-1 protein family strongly suggests that the Pvfp-1 functions as the byssal coating (lacquer) protein.

Adhesiveness↗
PubMed1981

Radiation-induced dimerization of tyrosine and glycyltyrosine in aqueous solutions.

Products of radiolysis of tyrosine and glycyl-L-tyrosine in oxygen-free nitrogen, N2O or air saturated water solution, pH 4.0 or 8.6 were analysed in an amino acid analyser and upon separation on DEAE cellulose or BioGel P-2 column with spectrofluorimetry. Apart from dihydroxyphenylalanine tyrosine solution irradiated in nitrogen or N2O contained dityrosine, while that of irradiated glycyl-L-tyrosine contained glycyl-dityrosine-glycine. Both dimeric products were formed with radiation yields, of about 0.15 at low pH value. In addition an unknown, nonfluorescent but ninhydrin positive product was found in irradiated tyrosine solution. Another, unidentified product of radiolysis was detected in N2O or air saturated solutions of tyrosine. The product had a blue-green fluorescence and a molecular weight of about 500.

Cobalt Radioisotopes↗
PubMed1991

[Determination of 2,6-diaminopimelic acid in swine feces and chymus].

A method is described for estimation of 2.6-diaminopimelic acid (DAP) using an automated amino acid analyzer and MOORE and STEIN ninhydrin reagent. Investigations were made concerning the influence of sample treatment on DAP content of faeces and ileal digesta of pigs and isolated bacteria. Oxidation before hydrolysis did not change DAP content of faeces and bacterial samples, but increased DAP of digesta. Since analytical reasons were excluded, different accessibility of DAP in faeces and digesta for hydrolysis is suggested. Lyophilization or preservation of fresh samples with formaldehyde and phenolic solution, resp., resulted in no significant influence on DAP content.

Animals↗
PubMed1958

Morphological and chemical studies of the spores and parasporal bodies of Bacillus laterosporus.

Spores of Bacillus laterosporus were studied to determine the chemical and morphological nature of their basophilic canoe-shaped parasporal bodies. An unusually high phosphorus content of these spores compared to other Bacillus species appeared to be associated with the parasporal body. Preparations of these "canoes" still attached to the spore coats were indeed high in phosphorus, but also in nitrogen. They were free of lipide-soluble and nucleic acid phosphorus and stained for protein. Some 50 per cent of the total nitrogen, but only 6 to 10 per cent of the total P were liberated by extraction with alkali-thioglycollate (pH 11.5) or alkali alone (pH 12.2-12.5). Proteinaceous material was recovered from these alkaline extracts and electron microscopy indicated that there had been a marked loss of "canoe" substance. Extraction with acid, removed some 80 per cent of the phosphorus associated with the "canoes" as orthophosphate. Chromatographic analyses for amino acids indicated some 14 ninhydrin-positive spots in the canoe-coat preparations whereas the whole spores contained at least 16.

Acids↗
PubMed1972

Biosynthesis in isolated Acetabularia chloroplasts. I. Protein amino acids.

The ability of chloroplasts isolated from Acetabulana mediterranea to synthesize the protein amino acids has been investigated. When this chloroplast isolate was presented with (14)CO(2) for periods of 6-8 hr, tracer was found in essentially all amino acid species of their hydrolyzed protein Phenylalanine labeling was not detected, probably due to technical problems, and hydroxyproline labeling was not tested for The incorporation of (14)CO(2) into the amino acids is driven by light and, as indicated by the amount of radioactivity lost during ninhydrin decarboxylation on the chromatograms, the amino acids appear to be uniformly labeled. The amino acid labeling pattern of the isolate is similar to that found in plastids labeled with (14)CO(2) in vivo. The chloroplast isolate did not utilize detectable amounts of externally supplied amino acids in light or, with added adenosine triphosphate (ATP), in darkness. It is concluded that these chloroplasts are a tight cytoplasmic compartment that is independent in supplying the amino acids used for its own protein synthesis. These results are discussed in terms of the role of contaminants in the observed synthesis, the "normalcy" of Acetabularia chloroplasts, the synthetic pathways for amino acids in plastids, and the implications of these observations for cell compartmentation and chloroplast autonomy.

Acetabularia↗
PubMed1959

Enzyme biosynthesis in Escherichia coli.

Escherichia coli B synthesized beta-galactosidase and an enzyme system for D-xylose when exposed to lactose and xylose respectively in nitrogen-free media. The amount of beta-galactosidase formed in the absence of external nitrogen depended upon the nature of the medium in which the cells had originally been grown. Half as much of this enzyme was synthesized without exogenous nitrogen by cells taken from a nitrogen-rich medium as was formed by cells under favorable conditions with an external supply of nitrogen. Escherichia coli B contained a pool of nitrogen compounds soluble in 80 per cent ethanol and made up of several ninhydrin-positive components. One of these was identified chromatographically as glycine using an authentic radioactive sample. Another substance behaved like serine on the chromatograms. The internal pool of amino acids and peptides was large enough to account for the beta-galactosidase synthesized by cells exposed to lactose in a medium free of nitrogen. Some degree of interaction of the syntheses of the beta-galactosidase and xylose enzyme systems was observed in nitrogen-free media. This interaction produced a greater effect on the formation of beta-galactosidase and was attributed to a limiting factor(s) in the internal nitrogenous pool or to a limiting intermediate in enzyme synthesis.

Enzymes↗
PubMedDate not supplied

Immobilization of biomacromolecules onto aminolyzed poly(L-lactic acid) toward acceleration of endothelium regeneration.

By reaction of poly(L-lactic acid) (PLLA) membrane with 1,6-hexanediamine, free amino groups were introduced onto a PLLA surface, through which biocompatible macromolecules such as gelatin, chitosan, or collagen were covalently immobilized by employing glutaraldehyde as a coupling agent. The existence of free amino groups on the aminolyzed PLLA surface was verified quantitatively by the ninhydrin analysis method, which revealed that surface NH(2) density increased with 1,6-hexanediamine concentration or aminolyzing time. Scanning force microscopy measurements detected an increase in surface roughness after aminolysis. The culture of human umbilical vein endothelial cells (HUVECs) in vitro proved that the cell proliferation rate and cell activity of both aminolyzed and biomacromolecule-immobilized PLLAs were improved compared with control PLLA. Scanning electron microscopy observation showed more spreading and flat cell morphology after HUVECs were cultured for 4 days on either aminolyzed or biomacromolecule-immobilized PLLA membranes. Confluent cell layers were observed on the modified PLLA. Measurement of von Willebrand factor secreted by these HUVECs confirmed that endothelium function was maintained. Therefore, aminolysis and biomacromolecule immobilization are promising ways to accelerate endothelium regeneration, which is crucial for blood vessel tissue engineering.

Biocompatible Materials↗
PubMed1997

Plasma amino acid concentrations in elderly patients with protein energy malnutrition.

OBJECTIVE: to compare amino acid concentrations in healthy and malnourished elderly patients. METHOD: plasma amino acid concentrations were examined in 24 men and women (80-100 years of age) with protein energy malnutrition (PEM) and compared with those of 44 healthy, similarly-aged controls. Plasma samples were determined by using cation exchange columns with ninhydrin detection in an high performance liquid chromatography system. RESULTS: essential amino acid and non-essential amino acid plasma concentrations were significantly decreased in PEM (0.01 < P < 0.0001). Branched-chain amino acids and urea cycle amino acid plasma concentrations fell significantly (P < 0.0001). Plasma concentrations of alanine and glutamic acid + glutamine were also significantly reduced (P < 0.0001). CONCLUSIONS: in underweight elderly patients, the plasma amino acid pattern reflects the severity of the metabolic disturbance.

Aged↗