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Complete amino acid sequence of bovine colostrum low‐ M r cysteine proteinase inhibitor
Author(s) -
Hirado Masayuki,
Tsunasawa Susumu,
Sakiyama Fumio,
Niinobe Michio,
Fujii Setsuro
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81335-1
Subject(s) - thermolysin , colostrum , cysteine , cyanogen bromide , biochemistry , peptide sequence , chemistry , amino acid , digestion (alchemy) , enzyme , biology , chromatography , trypsin , antibody , gene , immunology
The complete amino acid sequence of bovine colostrum cysteine proteinase inhibitor was determined by sequencing native inhibitor and peptides obtained by cyanogen bromide degradation, Achromobacter lysylendopeptidase digestion and partial acid hydrolysis of reduced and S ‐carboxymethylated protein. Achromobacter peptidase digestion was successfully used to isolate two disulfide‐containing peptides. The inhibitor consists of 112 amino acids with an M r of 12787. Two disulfide bonds were established between Cys 66 and Cys 77 and between Cys 90 and Cys 110. A high degree of homology in the sequence was found between the colostrum inhibitor and human γ‐trace, human salivary acidic protein and chicken egg‐white cystatin.