Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
BINDING OF HEMOGLOBIN TO THE ENVELOPE OF PORPHYROMONAS-GINGIVALIS ANDISOLATION OF THE HEMOGLOBIN-BINDING PROTEIN
Autore:
FUJIMURA S; SHIBATA Y; HIRAI K; NAKAMURA T;
Indirizzi:
MATSUMOTO DENT COLL,DEPT ORAL MICROBIOL,HIROOKA GOBARA 1780 SHIOJIRI NAGANO 39907 JAPAN
Titolo Testata:
Infection and immunity
fascicolo: 6, volume: 64, anno: 1996,
pagine: 2339 - 2342
SICI:
0019-9567(1996)64:6<2339:BOHTTE>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
BLACK-PIGMENTED BACTEROIDES; HEMIN-BINDING; ACTINOBACILLUS-ACTINOMYCETEMCOMITANS; W50;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
S. Fujimura et al., "BINDING OF HEMOGLOBIN TO THE ENVELOPE OF PORPHYROMONAS-GINGIVALIS ANDISOLATION OF THE HEMOGLOBIN-BINDING PROTEIN", Infection and immunity, 64(6), 1996, pp. 2339-2342

Abstract

The binding activity of the Porphyromonas gingivalis envelope and hemoglobin was examined over a wide range of pH values from 4.5 to 9.0. The binding activity in low-pH buffers was much higher than that al high pH; the optimum pHs for the binding were found to be 4.5 and 5.0. Since the hemoglobin bound to the envelope was found to dissociate in the pH 8.5 and 9.0 buffers, the binding is reversible. We hypothesized that hemoglobin-binding protein (HbBP), responsible for the binding to hemoglobin, exists in the envelope and confirmed its presence by dot blot determination with peroxidase-conjugated hemoglobin. Then we attempted to isolate HbBP from the solubilized (by a detergent) materials of the envelope by affinity chromatography. The molecular mass of HbBP was 19 kDa, and the isoelectric point was 4.3.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 00:18:25