Complete amino acid sequence of bovine colostrum low‐ M r cysteine proteinase inhibitor
1985; Wiley; Volume: 186; Issue: 1 Linguagem: Inglês
10.1016/0014-5793(85)81335-1
ISSN1873-3468
AutoresMasayuki Hirado, Susumu Tsunasawa, Fumio Sakiyama, Michio Niinobe, Setsuro Fujii,
Tópico(s)Protein Hydrolysis and Bioactive Peptides
ResumoThe 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 Mr 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 gamma-trace, human salivary acidic protein and chicken egg-white cystatin.
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