Zobrazeno 1 - 10 of 13 pro vyhledávání: '"Marguerite Volini"'
3
Comparative properties of bovine heart and liver rhodaneses and the regulatory role of the rhodaneses in energy metabolism
Autor: Kathleen Ogata, Marguerite Volini
Publikováno v: Journal of Protein Chemistry. 5:239-246
In previous studies on the rhodanese activity of bovine liver mitochondria, we have shown that in addition to activity observed in the soluble protein fraction, there is rhodanese activity that is bound to the mitochondrial membrane. The latter activ
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3e05cc5f419b92a9472a75d1ac9c220e
https://doi.org/10.1007/bf01025422
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4
Rhodanese-iron protein association in bovine liver extracts
Autor: Marguerite Volini, Kathleen K. Ogata, Deborah Craven
Publikováno v: Biochemical and Biophysical Research Communications. 79:890-896
In semi-crude liver extracts, rhodanese is associated with iron protein. A component purified from mitochondrial extracts exhibits the properties of a rhodanese-apoprotein complex. It can be converted to a rhodanese-iron protein complex by incubation
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afe3dc29956fdfcb85759ca569077489
https://doi.org/10.1016/0006-291x(77)91194-9
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5
Studies on the Active Site of Rhodanese
Autor: Shu-Fang Wang, Marguerite Volini
Publikováno v: Journal of Biological Chemistry. 243:5465-5470
The complete loss of enzymic activity on reaction with alkylating agents, aromatic nitro compounds, or aliphatic mercaptans indicates the importance of sulfhydryl groups for catalysis. Analyses during the course of inactivation with any of these reag
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2d88e17f1b3335571b2eb740c610b692
https://doi.org/10.1016/s0021-9258(18)91969-1
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6
The Interdependence of Substrate and Protein Transformations in Rhodanese Catalysis
Autor: Shu-Fang Wang, Marguerite Volini
Publikováno v: Journal of Biological Chemistry. 248:7376-7385
The cationic site of the enzyme rhodanese forms ion pairs with the substrate and product anions, thiosulfate, cyanide, sulfite, and thiocyanate. It also forms ion pairs with such diverse anionic species as acetate, formate, sulfate, and glycinate. In
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09a596c8072d6d72b76a90d4b34b6aac
https://doi.org/10.1016/s0021-9258(19)43299-7
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8
The Mechanism of the Rhodanese-catalyzed Thiosulfate-Lipoate Reaction
Autor: John Westley, Marguerite Volini
Publikováno v: Journal of Biological Chemistry. 241:5168-5176
The individual reactions comprising the rhodanese-catalyzed thiosulfate-lipoate reaction were demonstrated kinetically. The mechanism was shown to be a reaction sequence in which the enzyme forms kinetically significant binary complexes with both thi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fb6963c1eea49ab825398b4c3b2b7d82
https://doi.org/10.1016/s0021-9258(18)96412-4
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9
Circular Dichroism Studies of Chymotrypsin and Its Derivatives
Autor: Marguerite Volini, Peter Tobias
Publikováno v: Journal of Biological Chemistry. 244:5105-5109
The kinetics of the deacylation of trimethylacetyl chymotrypsin were followed by direct observation of changes in the circular dichroism spectrum of the enzymic protein itself. These changes result either from an alteration of the protein conformatio
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d6a4afb45f3b52b84a5f8876adff5e6a
https://doi.org/10.1016/s0021-9258(18)63633-6
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