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TRYPTIC PEPTIDES FROM BOVINE WHITE MATTER PROTEOLIPIDS
Author(s) -
Chan David S.,
Lees Marjorie B.
Publication year - 1978
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1978.tb12390.x
Subject(s) - performic acid , amino acid , chemistry , biochemistry , digestion (alchemy) , peptide sequence , chromatography , peptide , gene
— The amino acid composition of the fractions obtained after tryptic digestion of performic acid oxidized and non‐oxidized white matter proteolipids was studied. The acid‐soluble fraction from the tryptic digest represented between 25 and 30% of the starting material and was relatively enriched in hydrophilic amino acids and deficient in hydrophobic amino acids. The acid‐soluble peptides were separated by high voltage paper electrophoresis, and the amino acid compositions of 16 peptides were determined; three additional peptides were obtained from the acid‐soluble digest of the oxidized proteolipid. The sequence of 7 peptides including the N‐ and C‐terminal peptides is reported. The results suggest that the protein is segregated into hydrophilic and hydrophobic regions and that small hydrophilic regions are separated by large hydrophobic areas.