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Titolo:
Iron protoporphyrin IX albumin complexing increases the capacity and avidity of its binding to the periodontopathogen Porphyromonas gingivalis
Autore:
Smalley, JW; Birss, AJ;
Indirizzi:
Univeyside,ool, Dept Clin Dent Sci, Oral Biol Unit, Liverpool L69 3BX, Mers Univ Liverpool Liverpool Merseyside England L69 3BX verpool L69 3BX, Mers
Titolo Testata:
MICROBIAL PATHOGENESIS
fascicolo: 3, volume: 26, anno: 1999,
pagine: 131 - 137
SICI:
0882-4010(199903)26:3<131:IPIACI>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-SERUM-ALBUMIN; HEMIN BINDING; PREVOTELLA-INTERMEDIA; HEMOGLOBIN-BINDING; LIPOTEICHOIC ACID; PROTEINS; DEGRADATION; VIRULENCE; W50; COMPONENTS;
Keywords:
Porphyromonas; binding; albumin; haemalbumin; periodontal disease; iron protoporphyrin IX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Smalley, JW Univeyside,ool, Dept Clin Dent Sci, Oral Biol Unit, Liverpool L69 3BX, Mers Univ Liverpool Liverpool Merseyside England L69 3BX 3BX, Mers
Citazione:
J.W. Smalley e A.J. Birss, "Iron protoporphyrin IX albumin complexing increases the capacity and avidity of its binding to the periodontopathogen Porphyromonas gingivalis", MICROB PATH, 26(3), 1999, pp. 131-137

Abstract

Cells of Porphyromonas gingivalis strains W50 and WPH35 bound albumin and haemalbumin complexes (with 2:1 and 1:1 molar ratios of protein to iron protoporphyrin IX) in a concentration-dependent manner. The binding capacity for both haemalbumins was greater than for albumin. Scatchard analysis of binding to strain W50 revealed monophasic binding for albumin with an association constant (K-a) similar to 10(5)/M. Binding of the haemalbumin complexes was biphasic. The K(a)s of the lower-affinity binding phases were similarto that for albumin, whilst those for the higher-affinity binding were approximately 20-30-fold greater. It is concluded that both the capacity and avidity for albumin binding to P. gingivalis are increased following haemalbumin complex formation. This phenomenon would enable cells to discriminate between albumin and haem-bearing albumin molecules as a potential source ofhaem. Such binding behaviour may confer a nutritional and ecological advantage in the periodontal pocket or gingival sulcus under conditions of haem limitation. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 10:26:12