scholarly journals Studies on Reduced Wool VI. Comparison of Peptides Containing S-Carboxymethylcysteinyl Residues in Different Protein Fractions

1965 ◽  
Vol 18 (6) ◽  
pp. 1227 ◽  
Author(s):  
IJ O'donnell ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Acid Hydrolysis ◽  
Aromatic Amino Acid ◽  
Protein Fractions ◽  
Cysteine Residues ◽  
Partial Acid Hydrolysis ◽  
Chromatographic Methods ◽  
Hydrolysis Of ◽  
Peptide Maps

Wool has been reduced and extracted by urea-mercaptoethanol solution and the cysteine residues labelled by carboxymethylation with 2-[14C]iodoacetate. The extracted protein has been fractionated into the three main classes of protein present in wool, namely the high-sulphur, low-sulphur, and high-glycine-high-aromatic amino acid fractions. After partial acid hydrolysis of each fraction, peptide maps were prepared by paper ionophoretic and chromatographic methods and the S-carboxymethyl- containing peptides located by radioautography. The peptide maps given by the three fractions were almost identical in the peptides obtained, although marked differences in intensities were apparent. However, radioautographs of peptide maps of tryptic digests of the three fractions showed marked differences in the peptide patterns obtained. The findings are discussed in relation to the structure and synthesis of wool.

A kinetic study of the acid autoxidation of tryptophan

1972 ◽  
Vol 25 (10) ◽  
pp. 2139 ◽  
Author(s):  
M Stewart ◽  
CH Nicholls
Keyword(s):  
Free Radical ◽  
Amino Acid ◽  
Kinetic Study ◽  
Acid Hydrolysis ◽  
Soda Glass ◽  
Glass Containers ◽  
Hydrolysis Of

The decomposition of tryptophan in aqueous HC1 at 100�C has been shown to proceed by a free-radical autoxidation mechanism. The acid functions by protonating the amino acid at either the 1- or 3-positions prior to autoxidation and so 1-methyltryptophan is also decomposed under these conditions. Impurities present in the soda glass containers used are shown to be responsible for the initiation of the reaction. The decomposition of tryptophan during the acid hydrolysis of proteins is considered in the light of these results.

Effect of bromide salts on the acid hydrolysis of anti-bacterial hydrophilic Schiff base amino acid iron(II) complexes

2014 ◽  
Vol 84 (10) ◽  
pp. 2037-2042 ◽  
Author(s):  
Ali M. Shaker ◽  
Lobna A. E. Nassr ◽  
Mohamed S. S. Adam ◽  
Ibrahim M. A. Mohamed
Keyword(s):  
Schiff Base ◽  
Amino Acid ◽  
Acid Hydrolysis ◽  
Hydrolysis Of

Phosphopeptides Obtained by Partial Acid Hydrolysis of α-Casein2

1957 ◽  
Vol 79 (10) ◽  
pp. 2559-2565 ◽  
Author(s):  
N. J. Hipp ◽  
M. L. Groves ◽  
T. L. McMeekin
Keyword(s):  
Acid Hydrolysis ◽  
Partial Acid Hydrolysis ◽  
Hydrolysis Of

scholarly journals The formation of lipid-linked sugars by cell-free preparations of lactating rabbit mammary gland

1978 ◽  
Vol 170 (3) ◽  
pp. 479-486 ◽  
Author(s):  
D A White
Keyword(s):  
Mammary Gland ◽  
Acid Hydrolysis ◽  
Alkaline Hydrolysis ◽  
Gel Electrophoresis ◽  
Incubation Medium ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein Fractions ◽  
Exogenous Substrate ◽  
Major Species ◽  
Hydrolysis Of

1. A lactating rabbit mammary-gland microsomal system catalysed the incorporation of mannose from GDP-[U-14C]mannose into three endogenous acceptors, (i) polyprenyl phosphate mannose, (ii) lipid-linked oligosaccharide and (iii) protein. 2. Synthesis of polyprenyl phosphate mannose was stimulated by addition of dolichol phosphate to the incubation medium and was reversed by addition of GDP. The product had properties identical with those of authentic dolichol phosphate mannose. 3. The oligosaccharides derived from acid hydrolysis of the lipid-linked oligosaccharide fraction were of six, eight and nine to ten monosaccharide units, the octasaccharide being the major species formed. The oligosaccharide appeared to be attached to the lipid via a pyrophosphate bridge, since strong alkaline hydrolysis liberated an oligosaccharide phosphate. 4. Polyprenyl phosphate mannose served as a mannose donor to lipid-linked oligosaccharides and protein. When added as exogenous substrate it gave rise to a lipid-linked oligosaccharide of about six units. 5. Incorporation of radioactivity in protein was low, but polyacrylamide-gel electrophoresis of the protein fractions indicated that polypeptides of mol.wts. 115000, 75000 and 33000 were labelled.

Correction for Amino Acid Loss during Acid Hydrolysis of a Purified Protein

1996 ◽  
Vol 236 (2) ◽  
pp. 199-207 ◽  
Author(s):  
Alison J. Darragh ◽  
Dorian J. Garrick ◽  
Paul J. Moughan ◽  
Wouter H. Hendriks
Keyword(s):  
Amino Acid ◽  
Acid Hydrolysis ◽  
Hydrolysis Of

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

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