Bovine seminal ribonuclease: Non-hyperbolic kinetics in the second reaction step |
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Authors: | Renata Piccoli Alberto Di Donato Sergej Dudkin Giuseppe D''Alessio |
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Affiliation: | Laboratoire de Radio-Immuno-Biochimie, UER Broussais-Hôtel-Dieu, 15, rue de l''Ecole de Médecine, 75270 Paris Cédex 06, France |
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Abstract: | Peroxisomes contain enzymes catalyzing the β-oxidation of fatty acids, which have been purified and partially characterized. Hypolipidemic drugs, including clofibrate, cause a marked proliferation of peroxisomes and a striking increase in the activity of their β-oxidation system. We have compared by sodium dodecyl sulfate—polyacrylamide gel electrophoresis the polypeptide patterns of normal and clofibrate-induced peroxisomes and the purified β-oxidation enzymes. The data allow a tentative identification of the β-oxidation enzymes among the peroxisomal polypeptides; these enzymes constitute only a small part of the protein of normal peroxisomes. A subset of peroxisomal polypeptides, including the β-oxidation enzymes, is preferentially increased by clofibrate. |
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Keywords: | BS-R Nase, bovine seminal ribonuclease R Nase A, bovine pancreatic R Nase A Cyd-P—Cyd, cytidine-3'-phosphate—5'-cytidine cyd-2',3'-P(cyclic), cytidine-2':3'- phosphate (cyclic) |
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