Bovine mitochondrial rhodanese is a phosphoprotein
نویسندگان
چکیده
منابع مشابه
Improved preparation of bovine liver rhodanese.
Chemical studies of rhodanese (thiosulfate : cyanide sulfurtransferase, EC 2.8.1.1) in this laboratory have prompted the development of a modified procedure for preparing the crystalline enzyme. The new method, which is based on the earlier procedure of S6rbo (1) as modified by Westley et al. (2-4), permits isolation in apparently monodisperse form of nearly 50% of the total rhodanese activity ...
متن کاملMitochondrial rhodanese: membrane-bound and complexed activity.
We have proposed that phosphorylated and dephosphorylated forms of the mitochondrial sulfurtransferase, rhodanese, function as converter enzymes that interact with membrane-bound iron-sulfur centers of the electron transport chain to modulate the rate of mitochondrial respiration (Ogata, K., Dai, X., and Volini, M. (1989) J. Biol. Chem. 204, 2718-2725). In the present studies, we have explored ...
متن کاملDimeric structure and zinc content of bovine liver rhodanese.
Evidence from gel filtration and sedimentation studies of crystalline bovine liver rhodanese indicated that the enzyme molecule of 37,000 molecular weight is a dimer. In the native state, this form is in rapid, pa-dependent equilibrium with the monomeric species. A stable dimer is formed under mild oxidizing conditions. Analysis of the protein by peptide mapping indicated that the monomers are ...
متن کاملAcid pH-induced conformational changes in bovine liver rhodanese.
The enzyme rhodanese is greatly stabilized in the range pH 4-6, and samples at pH 5 are fully active after several days at 23 degrees C. This is very different from results at pH greater than 7, where there is significant loss of activity within 1 h. A pH-dependent conformational change occurs below pH 4 in a transition centered around pH 3.25 that leads slowly to inactive rhodanese at pH 3 (t ...
متن کاملThe distribution of aspartic acid residues in bovine dentine phosphoprotein.
Recently, Weiner and Hood (Science 190:987989, 1975) reported the use of an acid hydrolysis procedure in the study of the aspartic acid linkages of the soluble protein of the organic matrix of mollusk shells. Peptide bonds on both sides of aspartic acid residues have been shown to be particularly labile to hydrolysis by dilute acetic or hydrochloric acids (SCHULTZ et al, Biochemistry 1:694-698,...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)81672-1