| FEBS Letters | |
| Complete amino acid sequence of bovine colostrum low‐M r cysteine proteinase inhibitor | |
| Fujii, Setsuro1  Sakiyama, Fumio1  Hirado, Masayuki1  Tsunasawa, Susumu1  Niinobe, Michio1  | |
| [1] Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan | |
| 关键词: Amino acid sequence; Cysteine proteinase inhibitor; Bovine colostrum; | |
| DOI : 10.1016/0014-5793(85)81335-1 | |
| 学科分类:生物化学/生物物理 | |
| 来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020286847ZK.pdf | 384KB |
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