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Titolo:
ALBUMIN AND HEMALBUMIN DEGRADATION BY PORPHYROMONAS-GINGIVALIS
Autore:
SMALLEY JW; BIRSS AJ;
Indirizzi:
UNIV LIVERPOOL,DEPT CLIN DENT SCI,ORAL BIOL UNIT,EDWARDS BLDG LIVERPOOL L69 3BX MERSEYSIDE ENGLAND
Titolo Testata:
Oral microbiology and immunology
fascicolo: 4, volume: 12, anno: 1997,
pagine: 254 - 258
SICI:
0902-0055(1997)12:4<254:AAHDBP>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-SERUM-ALBUMIN; EXTRACELLULAR MEMBRANE-VESICLES; TRYPSIN-LIKE-ENZYME; HEMIN-BINDING; BACTEROIDES-GINGIVALIS; PROTEASE ACTIVITY; W50; PROTEINS; PURIFICATION; HEMOPEXIN;
Keywords:
PORPHYROMONAS GINGIVALIS; HEMALBUMIN; ALBUMIN; PROTEASE; HEME;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
J.W. Smalley e A.J. Birss, "ALBUMIN AND HEMALBUMIN DEGRADATION BY PORPHYROMONAS-GINGIVALIS", Oral microbiology and immunology, 12(4), 1997, pp. 254-258

Abstract

Degradation of bovine albumin and hemalbumin by Porphyromonas gingivalis W50 cells under non-reducing conditions at 37 degrees C was examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and densitometry. Albumin and hemalbumins with heme:protein molar ratios of 1:1, 4:1 and 8:1 were degraded, yielding protease-resistant 55.6-kDa peptides. Cells of strains WPW 35, 11834, and Bg 381 also produced a similar digestion pattern. N-terminal sequencing of the 55.6-kDa albumindigestion fragment revealed two peptides with the sequences (82)glu-thr-tyr-gly-asp-met-ala and (95)gln-pro-glu-arg-asn-glu-cys, indicatingcleavage in the N-terminal hinge region. Tosyllysylchloromethylketoneand N-ethylmaleimide were the most effective in inhibiting breakdown of albumin and hemalbumin with a I:1 heme:protein ratio. Initial degradation rates of albumin and all hemalbumins were similar, but the total amount of hemalbumins degraded over 7.5 h decreased with increased ratio of bound hemin. The specific proteolysis of hemalbumin may enableP. gingivalis to release hemin from a region of the molecule where heme binding is least avid.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 15:59:31