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Titolo:
GTPASE PROPERTIES OF THE INTERFERON-INDUCED HUMAN GUANYLATE-BINDING PROTEIN-2
Autore:
NEUN R; RICHTER MF; STAEHELI P; SCHWEMMLE M;
Indirizzi:
UNIV FREIBURG,INST MED MIKROBIOL & HYG,ABT VIROL,HERMANN HERDER STR 11 D-79008 FREIBURG GERMANY UNIV FREIBURG,INST MED MIKROBIOL & HYG,ABT VIROL D-79008 FREIBURG GERMANY
Titolo Testata:
FEBS letters
fascicolo: 1, volume: 390, anno: 1996,
pagine: 69 - 72
SICI:
0014-5793(1996)390:1<69:GPOTIH>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
MESSENGER-RNAS; GMP;
Keywords:
INTERFERON; HUMAN; GTPASE; GTP HYDROLYSIS; GUANYLATE BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
13
Recensione:
Indirizzi per estratti:
Citazione:
R. Neun et al., "GTPASE PROPERTIES OF THE INTERFERON-INDUCED HUMAN GUANYLATE-BINDING PROTEIN-2", FEBS letters, 390(1), 1996, pp. 69-72

Abstract

Guanylate-binding proteins (GBPs) were originally described as proteins that are strongly induced by interferons and are capable of bindingto agarose-immobilized guanine nucleotides. hGBP1, the first of two members of this protein family in humans, was recently shown to represent a novel type of GTPase that hydrolyzes GTP predominantly to GMP. Wenow report that purified recombinant hGBP2 also hydrolyzes GTP very efficiently, although GDP rather than GMP was the major reaction product, The biochemical parameters of this reaction were as follows: K-m=313 mu M, turnover number=22 min(-1). Both hGBP1 and hGBP2 failed to hydrolyze GDP, however, GDP was an effective inhibitor of the hGBP2- but not the hGBP1-catalyzed GTP hydrolysis reaction. Thus, hGBP1 and hGBP2have similar biochemical properties, but show pronounced differences in product specificity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/01/20 alle ore 12:27:06