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Titolo:
HEMIN REGULATION OF HEMOGLOBIN BINDING BY PORPHYROMONAS-GINGIVALIS
Autore:
SMALLEY JW; BIRSS AJ; MCKEE AS; MARSH PD;
Indirizzi:
UNIV LIVERPOOL,DEPT CLIN DENT SCI,ORAL BIOL UNIT LIVERPOOL L69 3BX MERSEYSIDE ENGLAND PUBL HLTH LAB SERV,CTR APPL MICROBIOL & RES,DIV RES SALISBURY SP4 0JGWILTS ENGLAND
Titolo Testata:
Current microbiology
fascicolo: 2, volume: 36, anno: 1998,
pagine: 102 - 106
SICI:
0343-8651(1998)36:2<102:HROHBB>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACTEROIDES-GINGIVALIS; HEMOLYTIC-ACTIVITY; OUTER MEMBRANES; W50; PROTEINS; VIRULENCE; ENVELOPE; VESICLES; AFFINITY; GROWTH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
J.W. Smalley et al., "HEMIN REGULATION OF HEMOGLOBIN BINDING BY PORPHYROMONAS-GINGIVALIS", Current microbiology, 36(2), 1998, pp. 102-106

Abstract

Hemoglobin binding to chemostat-grown hemin-excess and hemin-limited cells of Porphyromonas gingivalis W50, and to cells of the avirulent, beige-pigmenting variant W50/BE1, was quantified. Hemin-excess W50 bound more hemoglobin than hemin-limited W50, mirroring the hemin-bindingability of these cells [Microb Ecol Health Dis 7:9-15, 1994]. In contrast to hemin, hemoglobin binding was not enhanced by sodium dithionite. The hemoglobin-binding capacity of hemin-excess W50/BE1 was below that of hemin-limited W50 and only observed under oxidizing conditions. Scatchard analysis revealed similar affinity constants for hemin-excess and hemin-limited W50, and confirmed a lower binding maximum for the latter. Hemin-excess WSO/BE1 displayed cooperative binding of hemoglobin. These differences in binding were reflected in the binding of a horse radish peroxidase-conjugated hemoglobin (HHRPO) in a dot-blot assay. However, neither the 32-kDa hemin-binding protein, nor its 19-kDaheat-modified form, from either hemin-limited W50 or hemin-excess W50/BE1, bound this conjugate. These data indicate that hemoglobin binding by P. gingivalis is hemin-regulated and occurs via a mechanism different from hemin binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 19:56:01