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Titolo:
CHARACTERIZATION OF THE HEPARIN-BINDING PROPERTIES OF HUMAN CLUSTERIN
Autore:
PANKHURST GJ; BENNETT CA; EASTERBROOKSMITH SB;
Indirizzi:
UNIV SYDNEY,DEPT BIOCHEM SYDNEY NSW 2006 AUSTRALIA UNIV SYDNEY,DEPT BIOCHEM SYDNEY NSW 2006 AUSTRALIA
Titolo Testata:
Biochemistry
fascicolo: 14, volume: 37, anno: 1998,
pagine: 4823 - 4830
SICI:
0006-2960(1998)37:14<4823:COTHPO>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
IMMUNE-COMPLEX FORMATION; MEMBRANE-ATTACK-COMPLEX; APOLIPOPROTEIN-J/CLUSTERIN; GROWTH-FACTOR; SULFATED GLYCOPROTEIN-2; TESTIS FLUID; HUMAN PLASMA; HUMAN-SERUM; PROTEIN; INHIBITOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
G.J. Pankhurst et al., "CHARACTERIZATION OF THE HEPARIN-BINDING PROPERTIES OF HUMAN CLUSTERIN", Biochemistry, 37(14), 1998, pp. 4823-4830

Abstract

Clusterin is a highly conserved mammalian glycoprotein which has beenpredicted to contain heparin-binding sites. We tested this predictionby studying the interactions between heparin and clusterin using ELISA and heparin affinity chromatography methodologies. Two forms of biotinylated heparin were used in ELISA: heparin which had been directly biotinylated with a biotin-N-hydroxysuccinimide ester and heparin whichhad been activated using epichlorohydrin and 1,6-diaminohexane prior to biotinylation. Both gave dose-dependent increases in ELISA signal with increasing concentrations of biotinylated heparin, with the lattergiving signals an order of magnitude greater than the former. There was a dose-dependent increase in the ELISA signal from bound biotinylated heparin with increasing concentrations of plate-bound clusterin. The apparent affinity constant for binding of biotinylated heparin to plate-bound clusterin at pH 6.0 was estimated as 0.06 +/- 0.02 mu M. Unlabeled heparin blocked the binding of biotinylated heparin to clusterin over a concentration range similar to that of the binding of biotinylated heparin to plate-bound clusterin. The binding of biotinylated heparin to clusterin was independent of the presence or absence of Ca2+. The binding of biotinylated heparin to plate-bound clusterin increased with decreasing pH over the range 5.5-8.0 and was characterized by an apparent pK(a) of 6.9. Clusterin in human serum bound to heparin-Sepharose at pH 6.0 but not at pH 7.4. Dot-blot experiments showed that one of the polypeptide chains of clusterin which had been reduced and alkylated under denaturing conditions bound to heparin-Sepharose. This chain was identified as the a chain from its N-terminal amino acid sequence.

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Documento generato il 05/12/20 alle ore 14:00:44