Purification and characterization of the nickel-containing multicomponent urease from Klebsiella aerogenes.
1987; Elsevier BV; Volume: 262; Issue: 13 Linguagem: Inglês
10.1016/s0021-9258(18)45522-6
ISSN1083-351X
AutoresMatthew J. Todd, Robert P. Hausinger,
Tópico(s)Enzyme Production and Characterization
ResumoKlebsiella aerogenes urease was purified 1,070-fold with a 25% yield by a simple procedure involving DEAE-Sepharose, phenyl-Sepharose, Mono Q , and Superose 6 chromatographies.The enzyme preparation was comprised of three polypeptides with estimated M, = 72,000, 11,000, and 9,000 in a ad474 quaternary structure.The three components remained associated during native gel electrophoresis, Mono Q chromatography, and Superose 6 chromatography despite the presence of thiols, glycols, detergents, and varied buffer conditions.The apparent compositional complexity of K .aerogenes urease contrasts with the simple well-characterized homohexameric structure for jack bean urease (Dixon, N.
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