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Titolo:
BIOLOGICAL AND ANTIGENIC CHARACTERIZATION OF 3 BAPNA-HYDROLYZING PROTEASES FROM THE CULTURE SUPERNATANT OF PORPHYROMONAS-GINGIVALIS
Autore:
HINODE D; MASUDA K; YOSHIOKA M; HAYASHI H; NAKAMURA R; GRENIER D; MAYRAND D;
Indirizzi:
UNIV LAVAL,FAC MED DENT,GRP RECH ECOL BUCCALE ST FOY PQ G1K 7P4 CANADA UNIV TOKUSHIMA,SCH DENT,DEPT PREVENT DENT TOKUSHIMA 770 JAPAN
Titolo Testata:
Oral microbiology and immunology
fascicolo: 1, volume: 11, anno: 1996,
pagine: 8 - 14
SICI:
0902-0055(1996)11:1<8:BAACO3>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACTEROIDES-GINGIVALIS; COLLAGENASE ACTIVITY; PRTC GENE; HEMAGGLUTININ; W50; PURIFICATION; MEMBRANES; SEQUENCE; PROTEINS; CLONING;
Keywords:
PORPHYROMONAS GINGIVALIS; BAPNA-HYDROLYZING PROTEASE; PERIODONTAL DISEASE; PATHOGENICITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
42
Recensione:
Indirizzi per estratti:
Citazione:
D. Hinode et al., "BIOLOGICAL AND ANTIGENIC CHARACTERIZATION OF 3 BAPNA-HYDROLYZING PROTEASES FROM THE CULTURE SUPERNATANT OF PORPHYROMONAS-GINGIVALIS", Oral microbiology and immunology, 11(1), 1996, pp. 8-14

Abstract

Biological and antigenic distinction of 3 N alpha-benzoyl-DL-argininep-nitroanilide (BApNA)-hydrolyzing proteases (Pase-B, Pase-C and Pase-S) isolated from the culture supernatant of Porphyromonas gingivalis were determined. Immunoblotting analysis of these enzymes using a polyclonal antibody against Pase-S, which is a soluble, clostripain-like protease, revealed immunological distinction from Pase-C, a vesicle-associated thiol-protease. Pase-B, a vesicle-associated clostripain-like protease, reacted with the antibody and was also found to contain a considerable amount of carbohydrates in its structure, as compared with the others. Analysis of N-terminal amino acids of Pase-B provided a sequence not found in the SwissProt data bank or previously reported as N-terminal sequences of proteases from P. gingivalis. Pase-S, resembling Pase-B in its hydrolytic specificity, cleaved only arginine residues of peptides and degraded type IV and denatured type I collagen. Pase-C hydrolyzed Na-benzoyl-DL-lysine p-nitroanilide and showed the strongest capacity of degrading native type I collagen. This enzyme was also the only one to possess hemagglutinating activity. Our findings suggest that Pase-S from P. gingivalis is less active than Pase-C and thatthe enzyme may be an isozyme of Pase-B.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 16:45:28