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Titolo:
Bombyx cysteine proteinase inhibitor (BCPI) homologous to propeptide regions of cysteine proteinases is a strong, selective inhibitor of cathepsin L-like cysteine proteinases
Autore:
Kurata, M; Yamamoto, Y; Watabe, S; Makino, Y; Ogawa, K; Takahashi, SY;
Indirizzi:
Yamaguchi Univ, Fac Agr, Dept Vet Sci, Lab Biochem & Radiat Biol, Yamaguchi 7538515, Japan Yamaguchi Univ Yamaguchi Japan 7538515 at Biol, Yamaguchi 7538515, Japan Yamaguchi Univ, Sch Med, Dept Hlth Sci, Yamaguchi 7538505, Japan YamaguchiUniv Yamaguchi Japan 7538505 lth Sci, Yamaguchi 7538505, Japan Natl Inst Basic Biol, Ctr Analyt Instruments & Radioisotope Facil, Okazaki, Aichi 4448585, Japan Natl Inst Basic Biol Okazaki Aichi Japan 4448585 ki, Aichi 4448585, Japan
Titolo Testata:
JOURNAL OF BIOCHEMISTRY
fascicolo: 6, volume: 130, anno: 2001,
pagine: 857 - 863
SICI:
0021-924X(200112)130:6<857:BCPI(H>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
SLOW-BINDING; PROCATHEPSIN-B; CYSTATIN-C; PROTEASE; ENZYME; PROREGION; PAPAIN; EGGS; MORI; PURIFICATION;
Keywords:
Bombyx; cathepsin L; cysteine proteinase; inhibitor; propeptide;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Yamamoto, Y Yamaguchi Univ, Fac Agr, Dept Vet Sci, Lab Biochem & Radiat Biol, Yamaguchi 7538515, Japan Yamaguchi Univ Yamaguchi Japan 7538515 aguchi 7538515, Japan
Citazione:
M. Kurata et al., "Bombyx cysteine proteinase inhibitor (BCPI) homologous to propeptide regions of cysteine proteinases is a strong, selective inhibitor of cathepsin L-like cysteine proteinases", J BIOCHEM, 130(6), 2001, pp. 857-863

Abstract

Bombyx cysteine proteinase inhibitor (BCPI) is a novel cysteine proteinaseinhibitor. The protein sequence is homologous to the proregions of certaincysteine proteinases. Here we report the mechanism of its inhibition of several cysteine proteinases. BCPI strongly inhibited Bombyx cysteine proteinase (BCP) activity with a K-i = 5.9 muM, and human cathepsin L with a K-i =36 muM. The inhibition obeyed slow-binding kinetics. The inhibition of cathepsin H was much weaker (K-i = 82 nm), while inhibition of papain (K-i > 1muM) and cathepsin B (K-i > 4 muM) was negligible. Following incubation with BCP, BCPI was first truncated at the C-terminal end, and then gradually degraded over time. The truncation mainly involved two C-terminal amino acid residues. Recombinant BCPI lacking the two C-terminal amino acid residuesstill retained substantial inhibitory activity. Our results indicate that BCPI is a stable and highly selective inhibitor of cathepsin L-like cysteine proteinases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/04/20 alle ore 09:45:53