Structural studies on bovine  -crystallin.
The amino acid sequences around the cysteine residues in the lens protein, gamma-crystallin, were studied. Fraction II of the gamma-crystallin from calf lens (Björk, 1964) was used. The protein was oxidized with performic acid and then hydrolysed with trypsin. Six peptides containing cysteic acid were isolated. One of the peptides contained three residues of cysteic acid and the others contained one residue of cysteic acid. We conclude that there are eight unique residues of cysteic acid in the oxidized protein. Amino acid analysis suggests that there are also eight residues of cysteic acid in the molecule, which thus contains only one polypeptide chain.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D002854:Chromatography, Paper; D003459:Crystallins / Q000032:analysis*; D003545:Cysteine / Q000032:analysis; D004586:Electrophoresis; D005561:Formates; D006868:Hydrolysis; D008961:Models, Structural; D008967:Molecular Biology; D010084:Oxidation-Reduction; D010455:Peptides / Q000032:analysis; D011506:Proteins; D014357:Trypsin
D003459:Crystallins; D005561:Formates; D010455:Peptides; D011506:Proteins; D014357:Trypsin; D003545:Cysteine