Academic Journal
Purification of a nickel-containing urease from the rumen anaerobe Selenomonas ruminantium.
| Τίτλος: | Purification of a nickel-containing urease from the rumen anaerobe Selenomonas ruminantium. |
|---|---|
| Συγγραφείς: | Hausinger RP |
| Πηγή: | The Journal of biological chemistry [J Biol Chem] 1986 Jun 15; Vol. 261 (17), pp. 7866-70. |
| Τύπος έκδοσης: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| Imprint Name(s): | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| Ιατρικοί όροι (MeSH): | Gram-Negative Anaerobic Bacteria/*enzymology , Nickel/*analysis , Rumen/*microbiology , Urease/*isolation & purification, Urease/metabolism ; Anaerobiosis ; Animals ; Cattle ; Kinetics ; Macromolecular Substances ; Molecular Weight |
| Περίληψη: | Urease was purified 592-fold to homogeneity from the anaerobic rumen bacterium Selenomonas ruminantium. The urease isolation procedure included a heat step and ion-exchange, hydrophobic, gel filtration, and fast protein liquid chromatography. The purified enzyme exhibited a Km for urea of 2.2 +/- 0.5 mM and a Vmax of 1100 mumol of urea min-1 mg-1. The molecular mass estimated for the native enzyme was 360,000 +/- 50,000 daltons, whereas a subunit value of 70,000 +/- 2,000 daltons was determined. These results are in contrast to the findings of Mahadevan et al. (Mahadevan, S., Sauer, F. D., and Erfle, J. D. (1977) Biochem. J. 163, 495-501) in which isolated rumen urease was reported to be one-third this size (Mr 120,000-130,000) and to catalyze urea hydrolysis at a maximum velocity of only 53 mumol min-1 mg-1. S. ruminantium urease contained 2.1 +/- 0.4 nickel ions/subunit, comparable to the nickel content in jack bean urease (Dixon, N.E., Gazzola, C., Blakeley, R.L., and Zerner, B. (1975) J. Am. Chem. Soc. 97, 4131-4133). Thus, the active site of bacterial urease is very similar to that found in the plant enzymes. |
| Grant Information: | 2-507 RRO7049-15 United States RR NCRR NIH HHS |
| Substance Nomenclature: | 0 (Macromolecular Substances) 7OV03QG267 (Nickel) EC 3.5.1.5 (Urease) |
| Entry Date(s): | Date Created: 19860615 Date Completed: 19860709 Latest Revision: 20210210 |
| Update Code: | 20260130 |
| PMID: | 3711113 |
| Βάση Δεδομένων: | MEDLINE |
καταχωρήστε σχόλιο πρώτοι!