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 A study of the acidic peptides formed on the partial acid hydrolysis of wool

1949 ◽  
Vol 44 (5) ◽  
pp. 548-560 ◽  
Author(s):  
R. Consden ◽  
A. H. Gordon ◽  
A. J. P. Martin
Keyword(s):  
Acid Hydrolysis ◽  
Partial Acid Hydrolysis ◽  
Acidic Peptides ◽  
Hydrolysis Of

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.

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