Author/Editor | Turk, B; Ritonja, A; Bjork, I; Stoka, V; Dolenc, I; Turk, V | |
Title | Identification of bovine stefin A, a novel protein inhibitor of cysteine proteinases | |
Type | članek | |
Source | Febs Lett | |
Vol. and No. | Letnik 360, št. 2 | |
Publication year | 1995 | |
Volume | str. 101-5 | |
Language | eng | |
Abstract | For the first time, three different stefins, A, B and C, have been isolated from a single species. The complete amino acid sequence of bovine stefin A was determined. The inhibitor, with a calculated M(r) of 11,123, consists of 98 amino acid residues. Although it exhibits considerable similarity to human and rat stefin A, some significant differences in inhibition kinetics were found. Bovine stefin A bound tightly and rapidly to cathepsin L (kass = 9.6 x 10(6) M-1.s-1, Ki = 29 pM). The binding to cathepsin H was also rapid (kass = 2.1 x 10(6) M-1.s-1), but weaker (Ki = 0.4 nM) due to a higher dissociation rate constant. In contrast, the binding to cathepsin B was much slower (kass = 1.4 x 10(5) M-1.s-1), but still tight (Ki = 1.9 nM). | |
Descriptors | CYSTATINS CYSTEINE PROTEINASE INHIBITORS AMINO ACID SEQUENCE CATHEPSINS CATTLE KINETICS MOLECULAR SEQUENCE DATA SEQUENCE ALIGNMENT SEQUENCE HOMOLOGY, AMINO ACID SKIN |