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[Electrolytic coloration and spectral property of potassium bromide crystals].

Potassium bromide crystals were effectively colored electrolytically with a lab-made electrolytic apparatus at 693 K by applying a DC 1 200 V voltage. A lot of F, R, M and N type and some new unknown color centers were produced in the colored potassium bromide crystals, and the formation and transformation mechanisms of the color centers were presented. Spectral measurement and analysis were carried out systematically for the colored crystals, the spectral bands of corresponding color centers were reasonably resolved from the measured spectra, and the corresponding spectral parameters of the spectral bands were accurately determined by using spectral decomposition.

Bromides↗

The primary structure of human plasma high density apolipoprotein glutamine I (ApoA-I). II. The amino acid sequence and alignment of cyanogen bromide fragments IV, III, and I.

Apolipoprotein glutamine I (apoLP-Gln-I or apoA-I) is the major protein constituent of the human plasma high density lipoproteins. Cleavage of this protein with cyanogen bromide yields four fragments, designated in the order of elution from Bio-Gel P-30 as CNBr I, II, III, and IV. In the first paper in this series, the amino acid sequence of the NH2-terminal fragment, CNBr II, is reported. In the present study, CNBr IV, III, and I, containing, respectively, 25, 36, and 94 amino acids were sequenced by conventional means. To establish the alignment of the cyanogen bromide fragments, apoLP-Gln-I was digested with trypsin and two of the three methionine-containing tryptic peptides were isolated. The amino acid sequence of apoLP-Gln-I is as follows: (see article). With the complete amino acid sequence available, a CPK space-filling model of apoLP-Gln-I was constructed. The protein was placed into an alpha helical conformation wherever the primary structure permitted. Thirteen helical regions were identified. These regions account for 70% of the amino acid residues of the protein. Each helix is characterized as having two faces (amphipathic). One is a polar face that occupies approximately 180 degrees of the surface of the helix and the other is a hydrophobic face that occupies the other 180 degrees of the helical surface. Similar amphipathic helices have been identified previously in the other lipoprotein-proteins that have known sequences. It is suggested that the amphipathic helical regions of apoLP-Gln-I are important in the binding of phospholipids in high density lipoproteins.

Amino Acid Sequence↗

[Long-acting m-cholinolytic thiotropium bromide (spiriva) in therapy of patients with chronic obstructive pulmonary disease (stage 3)].

AIM: To elicit efficacy of a 3-month treatment with new inhaled cholinolytic drug spiriva in patients with chronic obstructive pulmonary disease (COPD) of stage 3. MATERIAL AND METHODS: Clinical symptoms (a total score of symptoms), external respiration function (ERF), pressure in the pulmonary artery were examined in 28 patients with COPD (stage 3). RESULTS: Long-acting thiotropium bromide relieved symptoms (the score decreased from 7.8 +/- 0.4 to 5.6 +/- 0.5), respiratory capacity rose from 68.8 +/- 2.4% to 75.9 +/- 2.5%, forced expiratory volume per 1 s increased from 41.9 +/- 2.6% to 46.6 +/- 3.2%, mean pressure in the pulmonary artery lowered from 29.0 +/- 0.8 to 25.1 +/- 1.2 mm Hg. CONCLUSION: Regular therapy with long-acting thiotropium bromide in patients with COPD stage 3 reduces clinical symptoms: dyspnea, mean pressure in the pulmonary artery. It also improves bronchial permeability.

Administration, Inhalation↗

Subchronic oral toxicity of pyridostigmine bromide in rats.

This study evaluated the oral toxicity of pyridostigmine bromide in Sprague-Dawley rats when administered for 13 weeks by daily gavage. Groups of 10 rats/sex received doses of 0, 5, 15, 30, or 60 mg/kg/day. Toxicity was limited to exaggerated cholinergic stimulation at doses of 15 mg/kg/day or greater. Significant findings included tremors and inhibition of RBC acetylcholinesterase. Thus, 5 mg/kg/day of pyridostigmine bromide appears to be the no observed toxic effect level under the conditions of the present investigation.

Administration, Oral↗

The effect of repeated doses of 30 mg pyridostigmine bromide on pilot performance in an A-4 flight simulator.

The effect of repeated doses of 30 mg pyridostigmine bromide every 8 h on flight skills in an A-4 simulator was tested in this crossover double-blind placebo-controlled study on 10 pilots experienced in actual and simulated A-4 flights. The pilots flew two test simulator flights 2 h after the fourth dose of pyridostigmine or placebo. The flight profile included navigation, rapid ascent, 360 degrees turns, and instrument landing. Each flight lasted approximately 20 min. Flight parameters measured included indicated air speed, true heading, barometric altitude, vertical velocity, and bank. The mean whole blood cholinesterase inhibition level was 29%. There was no decrement in performance under treatment with pyridostigmine in the percent of deviation time from the prescribed limits or in the average duration or magnitude of the deviation in each of the flight parameters. We conclude that pyridostigmine bromide in repeated doses of 30 mg every 8 h does not appear to influence pilot performance during short A-4 missions.

Adult↗

The amino acid sequence of fragment A, an enzymically active fragment of diphtheria toxin. II. The cyanogen bromide peptides.

Cyanogen bromide cleavage of Fragment A from diphtheria toxin at the four methionines present in each molecule resulted in five major peptides which were isolated and studied by sequence methods. These five peptides of 4, 11, 14, 63, and 101 residues account for all 193 residues in Fragment A and provide overlaps for the tryptic peptides from the maleylated protein. Two additional peptides were isolated and shown to be shorter forms (8 and 10 residues) of the COOH-terminal cyanogen bromide peptide (11 residues).

Adenosine Diphosphate Sugars↗

Single-crystal EPR study of novel azide complex of cyanogen bromide-modified myoglobin. Influence of specific modification of the heme distal histidyl residue on the ligand-binding structure.

Stable azide complex of cyanogen bromide-modified met-myoglobin (metMb) was prepared and crystallized. The principal values and eigen vectors of g-tensor were determined by single-crystal EPR spectroscopy at 77 K: gxx = 1.50, gyy = 2.32, and gzz = 2.91. These g values were similar to those of tetrazole derivative rather than azide derivative of native metMbs, suggesting that tetrazole derivative might be formed from N-cyanoimidazole of distal histidyl residue via nucleophilic attack of azide ion by 1,3-dipolar cycloaddition reaction. The orientation of the maximal g value (gzz) of the novel product was found to deviate about 13 degrees from the heme normal of native aquometMb. Thus, the orientation of the heme plane might be altered in passing from native metMb to cyanogen bromide-mediated metmyoglobin. The present EPR results demonstrated that the modification of the histidyl residue at the heme distal side causes the changes in the stereochemical and electronic natures of the ligand binding to the heme.

Azides↗

Different sensitivity of beta 1- and beta 2-adrenergic receptors towards cyanogen bromide.

beta 1-Adrenergic receptors of turkey and beta 2-receptors of rat erythrocyte membranes were identified by (-)-[3H]-dihydroalprenolol ([3H]-DHA) binding. Treatment of these membranes with the reagent cyanogen bromide causes a concentration dependent decrease in the number of binding sites, without affecting the affinity of the tracer. Whereas inactivation of the beta 1-receptors is not affected by the pH (between pH 6 and 9), substantial inactivation of the beta 2-receptors takes place only under mild acidic conditions. The ability of CNBr (cyanogen bromide) to discriminate between both receptor subclasses at basic pH is also confirmed for rat heart membranes (beta 1-receptors), Friend erythroleukemia and S49 lymphoma cell membranes (beta 2-receptors).

Animals↗

[Use of vecuronium bromide administered at a constant rate during renal transplantation].

The authors describe a technique of vecuronium bromide perfusion at constant flow used to obtain curarisation during 50 renal transplantations. The muscular effects of the drug were monitored through an electromyographical recorder, so as to adjust the perfusion rate. The dose of vecuronium bromide was 47.7 +/- 0.74 micrograms X kg-1 X h-1 (mean +/- SEM), this being lower than the dose recommended by D'Hollander (60 micrograms X kg-1 X h-1) for patients with normal renal function. Furthermore, no recurarisation was observed. Therefore, vecuronium can be considered as a satisfactory muscle relaxant in patients with renal failure, but neuromuscular monitoring appears to be a most important safety factor.

Adult↗

[Chemical reactions in double-stranded nucleic acids. IV. Cyanogen bromide--a highly effective reagent in the condensation of oligodeoxyribonucleotides].

Cyanogen bromide was found to induce a smooth and highly efficient condensation of oligonucleotide blocks within DNA duplexes. This template-directed reaction proceeds in the aqueous solution at 0 degree C for 1-2 min. Cyanogen bromide catalyzes the formation not only of phosphodiester, but also of unnatural phosphoramide and pyrophosphate interoligomer bonds.

Chemical Phenomena↗

Major proteins of the Escherichia coli outer cell envelope membrane. Sequence of the cyanogen bromide fragments of protein I from Escherichia coli B/r.

The sequence of the cyanogen bromide fragments of one of the major outer membrane proteins of E. coli B/r has been established with the aim of elucidating the primary structure of this protein. Separation of all fragments on one molecular sieve column was achieved upon citraconylation of these fragments. Overlapping peptides were obtained by digestion of the protein, or a cyanogen bromide fragment arising from incomplete cleavage, with trypsin or Staphylococcus aureus protease.

Amino Acid Sequence↗

[Isolation and characteristics of cyanogen bromide peptides of transducin alpha and beta subunits].

The alpha- and beta-subunits of the GTP-binding protein (transducin) from cattle retina were cleaved with cyanogen bromide. 21 peptides covering 90-100% of the amino acid sequence of the alpha- and beta-subunits were isolated from the hydrolyzate. Cyanogen bromide peptides complete or partial amino acid sequence was determined, the results were compared with those by Numa and coworkers [1] and Lochrie et al. [2] at the primary structure of the transducin alpha-subunit deduced from the nucleotide sequence of the cDNA. The structure by Lochrie is shown to differ much from the true structure of the alpha-subunit; probably, the investigators isolated cDNA, corresponding to the gene for some GTP-binding protein homologous to transducin, but not to the gene for the transducin alpha-subunit. The Numa's structure also contains an error. The final primary structure of the transducin alpha-subunit is given. The protein polypeptide chain consists of 349 amino acid residues and has an acetylmethionine residue as the N-terminal residue.

Amino Acid Sequence↗

[Primary structure of 20S,22R-cholesterol-hydroxylating cytochrome P-450 from bovine adrenal cortex mitochondria. IV. Structure of peptides of thermolytic and limited tryptic hydrolysis of the fragment F1; peptides of cyanogen bromide hydrolysis of cytochrome P-450. Complete amino acid sequence].

A thermolytic hydrolysis of maleinated fragment F1 has been performed, resulted in isolation of 44 peptides; their complete amino acid sequence has been determined. Non-overlapping thermolytic peptides of fragment F1 involve 178 amino acid residues, which comprises about 71% of its amino acid sequence. Also, the cleavage and structural investigation of some tryptophan-containing peptides obtained from the limited trypsinolysis of fragment F1 were carried out; reconstitution of the polypeptide chain of the fragment is completed. The cyanogen bromide cleavage of carboxymethylated cytochrome P-450 was achieved and 17 peptides, comprising almost the whole polypeptide chain of the protein molecule (91%), was isolated. To investigate structure of the cyanogen bromide peptides, we hydrolysed them at tryptophan residues with trypsin, chymotrypsin, proteinase from Staphylococcus aureus, and BNPS-skatole. The data obtained and those published earlier led to the complete primary structure of the cholesterol-hydroxylating cytochrome P-450. The proteins polypeptide chain consists of 481 amino acid residues and has the precise molecular mass 56 407.7.

Adrenal Cortex↗

Synthesis of long-chain alkyl and alkenyl bromides.

Long-chain alkyl and alkenyl bromides are obtained in quantitative yields by the reaction of methane-sulfonates with anhydrous magnesium bromide in absolute ether; cis-trans isomerization of double bonds does not occur.

Alkenes↗

[Primary structure of the elongation factor G from Escherichia coli. IX. Structure of peptides generated by cyanogen bromide cleavage of the G-factor isolated on thiol-activated sepharose and of the products of the G-factor cleavage at Asp-Pro bonds. Complete primary structure].

The amino acid sequence of cysteine- and cystine-containing peptides resulting from cleavage of the G-factor by cyanogen bromide has been determined. For structure analysis cyanogen bromide peptides were further degradated using trypsin, chymotrypsin, thermolysin, staphylococcal glutamic protease, or limited acid hydrolysis. The products of the G-factor cleavage at Asp-Pro bonds were also studied. The obtained data together with those published earlier permitted to establish the complete primary structure of the elongation factor G. The polypeptide chain consists of 701 amino acid residues and has molecular mass of 77321,46.

Amino Acid Sequence↗

Histidine decarboxylase of Lactobacillus 30a. Sequences of the cyanogen bromide peptides from the alpha chain.

The alpha chain of histidine decarboxylase contains eight internal methionine residues. After reductive amination to convert the NH2-terminal pyruvoyl residue to an alanyl residue and cyanogen bromide treatment, 13 pure peptides were isolated. Four of these are incomplete cleavage products. The sequence of each of the remaining nine peptides was established by automated and manual degradation of the intact peptides and of smaller peptides obtained from tryptic, chymotryptic, and staphylococcal protease digests of the cyanogen bromide peptides. These results, together with the data on overlapping peptides reported in the accompanying paper (Huynh, Q. K., Recsei, P. A., Vaaler, G. L., and Snell, E. E. (1984) J. Biol. Chem. 259, 2833-2839), establish the complete amino acid sequence of the alpha chain.

Amino Acid Sequence↗

[EEG changes in abuse and addiction of bromide hypnotics [author's transl)].

With bromism we stated a slow EEG-activity. Such alterations of the electro-encephalogram can be caused by urea of bromine, its metabolites and by the inorganic bromide ion. We tried to find out the real effect of the bromide ion which is not bound in the serum. Therefore we only examined the EEG and the bromine serum after the acute influence of the urea of bromine had faded (> 5 days). Patients suffering of disturbances of metabolism or system-diseases, tumors and infections or patients undergoing a medicamentous therapy were excluded from these tests. During the years 1971, 1972 and 1977 we found 26 patients (bromine in serum > 5 mg%) who corresponded to the above mentioned conditions and on whose data the results of our studies are based. 16 patients had very high bromine values (> 24,6 mg%). Most of these patients (10 out of 16) showed paranoid-hallucinatory symptoms. We also stated delirious and depressive attacks. No one suffered of mental dullness. The EEG of 7 patients showed general alterations. With lower bromine values (< 24,6 mg%) we could neither state general alterations of the EEG nor psychotic or delirious symptoms. We didn't observe any paroxysmal disturbance of the EEG. We also didn't notice a acceleration of the EEG, as it was stated with other medical preparations.

Adolescent↗

Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. I. Amino acid sequence of the cyanogen bromide peptides.

A histidine-rich fragment, Cp F5, with a molecular weight of 18,650 was isolated from human ceruloplasmin. It consists of 159 amino acids and contains a possible copper-binding site. The sequence of the first 18 NH2-terminal residues of Cp F5 was determined by automated Edman degradation. Cp F5 was cleaved by cyanogen bromide to produce nine fragments of from 2 to 63 residues. The amino acid sequence of all of the cyanogen bromide fragments was investigated using automated and manual Edman degradation, the fragments being digested with trypsin, chymotrypsin, thermolysin, staphylococcal protease, and pepsin as appropriate. The results, in conjunction with the data on the tryptic peptides reported in the accompanying paper (Kingston, I.B., Kingston, B.L., and Putnam, F.L. (1980) J. Biol. Chem. 255, 2886-2896), establish the complete amino acid sequence of Cp F5.

Amino Acid Sequence↗