1.
Boll Soc Ital Biol Sper
; 58(18): 1145-51, 1982 Sep 30.
Article
in English
| MEDLINE
| ID: mdl-6814469
ABSTRACT
Adenosine deaminase from Bacillus cereus is quite unstable, similarly to other bacterial deaminases, but it shows a peculiar stabilizing effect by some monovalent cations. These include K+, Li+, NH4+ and to a lesser extent Cs+. Maximal stabilization of the deaminase is exerted by K+ at concentrations higher than 20 mM. The enzyme can be rapidly inactivated by sulphydryl reagents such as p-hydroxymercuribenzoate. Since adenosine deaminase from B. cereus, in addition to monovalent cations, is stabilized also by dithiothreitol, a possible influence of monovalent cations on the reactivity of some sulphydryl groups on the enzyme has been suggested.
Subject(s)
Adenosine Deaminase/metabolism , Bacillus cereus/enzymology , Nucleoside Deaminases/metabolism , Animals , Calcium Chloride/pharmacology , Cattle , Hydroxymercuribenzoates/pharmacology , Kinetics , Magnesium/pharmacology , Magnesium Chloride , Potassium Chloride/pharmacology , Sodium Chloride/pharmacology , Time Factors
2.
Boll Soc Ital Biol Sper
; 42(19): 1352-4, 1966 Oct 15.
Article
in Italian
| MEDLINE
| ID: mdl-5972614