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Titolo:
PARTIAL-PURIFICATION OF AN IRON-DEPENDENT L-SERINE DEHYDRATASE FROM CLOSTRIDIUM-STICKLANDII
Autore:
ZINECKER H; ANDREESEN JR; PICH A;
Indirizzi:
UNIV HALLE WITTENBERG,INST MIKROBIOL,KURT MOTHES STR 3 D-06099 HALLE GERMANY UNIV HALLE WITTENBERG,INST MIKROBIOL D-06099 HALLE GERMANY
Titolo Testata:
Journal of basic microbiology
fascicolo: 2, volume: 38, anno: 1998,
pagine: 147 - 155
SICI:
0233-111X(1998)38:2<147:POAILD>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
PEPTOSTREPTOCOCCUS-ASACCHAROLYTICUS; SULFUR-CLUSTER; L-THREONINE; PROTEINS; SEQUENCE; ENZYMES; CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
H. Zinecker et al., "PARTIAL-PURIFICATION OF AN IRON-DEPENDENT L-SERINE DEHYDRATASE FROM CLOSTRIDIUM-STICKLANDII", Journal of basic microbiology, 38(2), 1998, pp. 147-155

Abstract

An oxygen-sensitive and highly unstable L-serine dehydratase was partially purified from the Grampositive anaerobe Clostridium sticklandii. The final active preparation contained five proteins of 27, 30, 44.5,46, and 58 kDa as judged by SDS-PAGE. The N-terminal sequence of the 30 kDa subunit showed some similarity to the a-subunits of the iron-containing L-serine dehydratases from Clostridium propionicum and Peptostreptococcus asaccharolyticus. Oxygen-inactivated L-serine dehy dratase from C. sticklandii was reactivated by incubation with Fe2+ under reducing conditions. Furthermore, the enzyme was inactivated by iron-chelating substances like phenanthroline and EDTA. Pyridoxal-5-phosphate (PLP) did not stimulate the activity, and known inhibitors of PLP-containing enzymes such as NaBH4 had no effect on the activity of L-serinedehydratase from C. sticklandii.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 06:00:28