scholarly journals Hydrolysis of the Peptide Bond and Amino Acid Modification with Hydriodic Acid

1971 ◽  
Vol 24 (4) ◽  
pp. 1235 ◽  
Author(s):  
AS Inglis ◽  
PW Nicholls ◽  
CM Roxburgh
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Boiling Point ◽  
Amino Acid Analysis ◽  
Peptide Bond ◽  
Hydriodic Acid ◽  
Acid Modification ◽  
Amino Acid Modification ◽  
Hydrolysis Of

Reaction of hydriodic acid with peptides and proteins has been studied. At the boiling point, hydrolysis of the peptide bond, particularly stable bonds linking valine and isoleucine residues, is facile. Several amino acids react with constantboiling hydriodic acid but the only reactions detrimental to the amino acid analysis are the reduction of serine with concomitant formation of alanine, and the destruction of tryptophan. Gentler conditions of hydrolysis with diluted hydriodic acid are required for analysis of serine. Good results for analysis of proteins for amino acids may be obtained after a 6-hr hydrolysis period.

A comparison of methods for determining the concentration of extracellular peptides in rumen fluid of sheep

1990 ◽  
Vol 114 (1) ◽  
pp. 101-105 ◽  
Author(s):  
R. J. Wallace ◽  
N. McKain
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Rumen Fluid ◽  
Amino Acid Content ◽  
Reliable Estimate ◽  
Precipitate Protein ◽  
Micro Organisms ◽  
Hydrolysis Of ◽  
Amino Acid Concentrations

SUMMARYSamples of rumen fluid were removed from pairs of sheep on four grass-hay-based diets 7 h after feeding. Micro-organisms were sedimented by centrifugation and the cell-free supernatant was treated with perchloric acid (PCA) to precipitate protein. The remaining fluid was analysed for peptides by several methods to determine how much peptide escaped degradation. Ammonia interfered with analysis by amino group reagents, especially ninhydrin. In this respect,o-phthalaldehyde and trinitrobenzene sulphonic acid were more specific and more useful than ninhydrin. Use of all these reagents showed that significant quantities of amino groups (equivalent to up to 153 mg amino acid N/1 of rumen fluid) were released by hydrolysis of the PCA extract with 6 M-HCI for 24 h. However, fluorescamine analysis indicated that the peptide content of the unhydrolysed PCA extract was < 3 mg N/1. The true amino acid content of different extracts was resolved by chromatographic amino acid analysis: the sum of individual amino acid concentrations in acid-hydrolysed PCA extracts of extracellular rumen fluid ranged from 7·8 to 14·5 mg N/1. Thus most of the free amino N released by hydrolysis of the PCA extract was not from amino acids, and most of the amino acids that were released were originally present in a form that did not react with fluorescamine. Although none of the methods gave a reliable estimate of peptide concentrations, amino acid analysis provided an upper limit. It was therefore concluded that peptide concentrations in extracellular rumen fluid are much lower than indicated by previous ninhydrin estimations, and that little dietary peptide escapes degradation for a prolonged period in the rumen.

D-Mannitol Interferes with Amino Acid Analysis of Marine Organisms

1979 ◽  
Vol 36 (9) ◽  
pp. 1134-1137 ◽  
Author(s):  
W. Fong ◽  
R. K. O'dor
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Hydrolysis ◽  
Key Words ◽  
Amino Acid Analysis ◽  
Chromatographic Analysis ◽  
Marine Algae ◽  
Protein S ◽  
New Compounds ◽  
Hydrolysis Of

Acid hydrolysis of a protein in the presence of D-mannitol, a common constituent of marine algae, can cause significant reductions in the recovery of a number of amino acids. The new compounds formed by the interactions of D-mannitol and these amino acids may interfere in the chromatographic analysis of other amino acids. The recoveries of most of the amino acids appear to be either directly or inversely proportional to the amount of D-mannitol added to a protein sample before acid hydrolysis. These results suggest that it is necessary to determine the effects of contaminants in a sample of protein(s) on the recoveries of amino acids during routine acid hydrolysis. Key words: kelp, amino acids, carbohydrates, D-mannitol

Improved purification and further characterization of Clostridium perfringens type A enterotoxin

1973 ◽  
Vol 19 (11) ◽  
pp. 1379-1382 ◽  
Author(s):  
A. H. W. Hauschild ◽  
R. Hilsheimer ◽  
W. G. Martin
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Clostridium Perfringens ◽  
Amino Acid Analysis ◽  
Sedimentation Coefficient ◽  
Type A ◽  
Sedimentation Equilibrium ◽  
Molecular Weights ◽  
Hydrolysis Of

The procedure for the purification of Clostridium perfringens type A enterotoxin was simplified, and the purity of the toxin was improved. Hydrolysis of the toxin by the p-toluenesulfonic acid procedure yielded 18 common amino acids. Among these, aspartic acid, serine, leucine, and glutamic acid were the predominant components. The sedimentation coefficient (s°20, w) was 2.8 Svedberg units. The molecular weights determined by the Archibald technique, sedimentation equilibrium, and amino acid analysis were 40 000, 36 000, and 33 000, respectively.

Hydrolysis of Proteins for Amino Acid Analysis. II. Acid Hydrolysis in Sealed Tubes of Mixtures of β-Lactoglobulin and Starch

1964 ◽  
Vol 47 (4) ◽  
pp. 745-747 ◽  
Author(s):  
William G Gordon ◽  
Jay J Basch
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Hydrolysis ◽  
Amino Acid Analysis ◽  
Special Method ◽  
Large Excess ◽  
Β Lactoglobulin ◽  
Hydrolysis Of

Abstract Experiments with a mixture of β-Iactoglobulin and starch, simulating the composition of carbohydrate-rich foods and feeds, have been carried out to determine conditions for acid hydrolysis that will permit maximal recovery of amino acids in hydrolysates of such materials. When a large excess of 6N HC1 is used for hydrolysis, good recoveries of most amino acids are obtained. However, about one-quarter of the tyrosine present is destroyed under the conditions investigated. Some destruction of methionine and cystine may also be attributed to the presence of carbohydrate, but a special method for the determination of these amino acids is available.

Two forms of poliovirus VPg result from amino acid modification of a single viral protein

Virology ◽  
1984 ◽  
Vol 136 (2) ◽  
pp. 453-456 ◽  
Author(s):  
Oliver C. Richards ◽  
Kathryn Morton ◽  
Susan C. Martin ◽  
Ellie Ehrenfeld
Keyword(s):  
Amino Acid ◽  
Viral Protein ◽  
Acid Modification ◽  
Amino Acid Modification

scholarly journals Isolation, purification and structure of exochelin MS, the extracellular siderophore from Mycobacterium smegmatis

1995 ◽  
Vol 305 (1) ◽  
pp. 187-196 ◽  
Author(s):  
G J Sharman ◽  
D H Williams ◽  
D F Ewing ◽  
C Ratledge
Keyword(s):  
Amino Acids ◽  
Mycobacterium Smegmatis ◽  
Methyl Esters ◽  
Three Dimensional ◽  
Iron Chelation ◽  
Peptide Bond ◽  
Exchange Chromatography ◽  
Peptide Bonds ◽  
Hydrolysis Of ◽  
Gallium Complex

The extracellular siderophore from Mycobacterium smegmatis, exochelin MS, was isolated from iron-deficiently grown cultures and purified to > 98% by a combination of ion-exchange chromatography and h.p.l.c. The material is unextractable into organic solvents, is basic (pI = 9.3-9.5), has a lambda max at 420 nm and a probable Ks for Fe3+ of between 10(25) and 10(30). Its structure has been determined by examination of desferri- and ferri-exochelin and its gallium complex. The methods used were electrospray-m.s. and one- and two-dimensional (NOESY, DQF-COSY and TOCSY) 1H n.m.r. The constituent amino acids were examined by chiral g.l.c analysis of N-trifluoroacetyl isopropyl and N-pentafluoropropionyl methyl esters after hydrolysis, and reductive HI hydrolysis, of the siderophore. The exochelin is a formylated pentapeptide: N-(delta-N-formyl,delta N-hydroxy-R-ornithyl) -beta-alaninyl-delta N-hydroxy-R-ornithinyl-R-allo-threoninyl-delta N-hydroxy-S-ornithine. The linkages involving the three ornithine residues are via their delta N(OH) and alpha-CO groups leaving three free alpha-NH2 groups. Although there are two peptide bonds, these involve the three R (D)-amino acids. Thus the molecule has no conventional peptide bond, and this suggests that it will be resistant to peptidase hydrolysis. The co-ordination centre with Fe3+ is hexadenate in an octahedral structure involving the three hydroxamic acid groups. Molecular modelling shows it to have similar features to other ferric trihydroxamate siderophores whose three-dimensional structures have been established. The molecule is shown to have little flexibility around the iron chelation centre, although the terminal (Orn-3) residue, which is not involved in iron binding except at its delta N atom, has more motional freedom.

Post-Translational Amino Acid Modification

2010 ◽  
pp. 1052-1052
Author(s):  
R. Hamish McAllister-Williams ◽  
Daniel Bertrand ◽  
Hans Rollema ◽  
Raymond S. Hurst ◽  
Linda P. Spear ◽  
...  
Keyword(s):  
Amino Acid ◽  
Acid Modification ◽  
Amino Acid Modification
Sign in / Sign up

Export Citation Format

Share Document