Dissociation of urease in acetate buffer of pH 3.5 with retention of the enzymatic activity
- PMID: 5705229
- DOI: 10.1007/BF02138313
Dissociation of urease in acetate buffer of pH 3.5 with retention of the enzymatic activity
Similar articles
-
A study of the structural subunits of urease obtained during controlled dissociation.Can J Biochem. 1972 May;50(5):461-73. doi: 10.1139/o72-064. Can J Biochem. 1972. PMID: 5028152 No abstract available.
-
Dissociation of urease in aqueous 1,2-ethanediol.Biochem Biophys Res Commun. 1969 Sep 10;36(6):1045-52. doi: 10.1016/0006-291x(69)90310-6. Biochem Biophys Res Commun. 1969. PMID: 5344722 No abstract available.
-
[Investigation of association and dissociation in aspariginase solutions by ultracentrifugation].Biochim Biophys Acta. 1971 Apr 27;236(1):105-26. Biochim Biophys Acta. 1971. PMID: 4930862 German. No abstract available.
-
Jack bean urease (EC 3.5.1.5). Demonstration of a carbamoyl-transfer reaction and inhibition by hydroxamic acids.Biochemistry. 1969 May;8(5):1991-2000. doi: 10.1021/bi00833a032. Biochemistry. 1969. PMID: 5785219 No abstract available.
-
Acetic acid-urea polyacrylamide gel electrophoresis of proteins.Methods Mol Biol. 1994;32:39-47. doi: 10.1385/0-89603-268-X:39. Methods Mol Biol. 1994. PMID: 7951739 Review. No abstract available.
Cited by
-
Radiation-target molecular weights of urease and of L-glutamate dehydrogenase, and their relevance to the size of the functional subunits.Biochem J. 1971 May;122(5):677-80. doi: 10.1042/bj1220677. Biochem J. 1971. PMID: 5129263 Free PMC article.
-
The subunit structure of jack-bean urease.Biochem J. 1969 Jul;113(4):669-77. doi: 10.1042/bj1130669. Biochem J. 1969. PMID: 5386187 Free PMC article.