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Studies on the Primary Structure of Cow χ‐Casein.‐Structural Features of para‐χ‐Casein; N‐terminal sequence of χ‐caseinoglycopeptide studied with a sequencer
Author(s) -
Jollès Jacqueline,
Schoentgen Françoise,
Alais Charles,
Fiat AnneMarie,
Jollès Pierre
Publication year - 1972
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19720550820
Subject(s) - chemistry , casein , sequence (biology) , protein primary structure , glycopeptide , peptide sequence , peptide , amino acid residue , biochemistry , chromatography , gene , antibiotics
Several long tryptic peptides obtained from reduced maleylated χ‐casein were sequenced: they belonged to the N‐ and C‐terminal (37 residues) moieties of para‐χ‐casein. Several tryptic peptides could then be joined by chymotryptic overlap peptides. 102 amino acid residues of para‐χ‐casein were thus placed into two long and four shorter sequences. Some structural results were established with a Sequencer which was also employed for a verification of the N‐terminal sequence of the χ‐caseinoglycopeptide; a previously described short glycopeptide was found again and was reinvestigated.