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