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Titolo:
HEMOGLOBIN-BINDING PROTEIN PURIFIED FROM PORPHYROMONAS-GINGIVALIS IS IDENTICAL TO LYSINE-SPECIFIC CYSTEINE PROTEINASE (LYS-GINGIPAIN)
Autore:
KUBONIWA M; AMANO A; SHIZUKUISHI S;
Indirizzi:
OSAKA UNIV,FAC DENT,DIV SPECIAL CARE DENT,1-8 YAMADAOKA SUITA OSAKA 5650871 JAPAN OSAKA UNIV,FAC DENT,DIV SPECIAL CARE DENT SUITA OSAKA 5650871 JAPAN OSAKA UNIV,FAC DENT,DEPT PREVENT DENT SUITA OSAKA 565 JAPAN
Titolo Testata:
Biochemical and biophysical research communications (Print)
fascicolo: 1, volume: 249, anno: 1998,
pagine: 38 - 43
SICI:
0006-291X(1998)249:1<38:HPPFPI>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
HEMIN-BINDING; ARG-GINGIPAIN; PATHOGENIC BACTERIA; MOLECULAR-CLONING; SURFACE PROTEIN; MATRIX PROTEINS; IRON TRANSPORT; LIMITATION; GROWTH; W50;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
M. Kuboniwa et al., "HEMOGLOBIN-BINDING PROTEIN PURIFIED FROM PORPHYROMONAS-GINGIVALIS IS IDENTICAL TO LYSINE-SPECIFIC CYSTEINE PROTEINASE (LYS-GINGIPAIN)", Biochemical and biophysical research communications (Print), 249(1), 1998, pp. 38-43

Abstract

The functional protein that binds to human hemoglobin (hemoglobin-binding protein; HBP) was purified from Porphyromonas gingivalis cells. The analyses of the amino-terminal sequence and amino acid composition revealed that HBP is identical to lysine-specific cysteine proteinase (51 kDa Lys-gingipain; KGP) of P. gingivalis 381. It is a novel finding that KGP has binding affinity to hemoglobin. The binding activity ofHBP was enhanced by acidic or anaerobic conditions. Arg-gingipain, a member of the gingipain family, of P. gingivalis exhibited no ability to bind to hemoglobin. The recombinant protein of KGP (r-KGP) generated in Escherichia coli showed both hemoglobin-binding and proteolytic activities. The treatment of r-KGP by protein disulfide isomerase effectively enhanced binding to hemoglobin, whereas the proteinase activitywas decreased. The treated r-KGP significantly inhibited the binding of hemoglobin to the whole cell extracts in a dose-dependent manner. These results suggest that the hemoglobin binding of P. gingivalis is mediated by KGP through active domain(s) distinct from that for proteinase activity. (C) 1998 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 15:42:26