Modification of leucine dehydrogenase by pyridoxal 5'-phosphate.
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چکیده
منابع مشابه
Reversible modification of pig heart mitochondrial malate dehydrogenase by pyridoxal 5'-phosphate.
1. Pig heart mitochondrial malate dehydrogenase incubated with pyridoxal 5'-phosphate at pH 8.0 and 25 degrees C gradually loses activity. Such inactivation can be largely reversed by dialysis or by addition of L-lysine or L-cysteine, and can be made permanent by NaBH4 reduction. 2. Modification of malate dehydrogenase with pyridoxal 5'-phosphate at 35 degrees C involves two phases, an initial ...
متن کاملBinding of Pyridoxal 5'-Phosphate
1. The a and ,B subforms of aspartate aminotransferase were purified from pig heart. 2. The a subform contained 2mol of pyridoxal 5'-phosphate. The apo-(a subform) could be fully reactived by combination with 2mol of cofactor. 3. The protein fluorescence of the apo(a subform) decreased non-linearly with increase in enzyme activity and concentration of bound cofactor. 4. It is concluded that the...
متن کاملModification of pepsinogen with pyridoxal phosphate.
Pyridoxal-PO* binds to pepsinogen in a reaction in which the stoichiometry is highly dependent on the conformation of the protein. When pepsinogen is in its native conformation, pyridoxal-PO4 forms Schiff bases with the (r-NH2 group of Leul and the e-NH2 group of LysZS8. When the protein is mildly denatured and assumes a more extended conformation, pyridoxal-PO4 can react with the t-NH2 groups ...
متن کاملInactivation of porcine heart cytoplasmic malate dehydrogenase by pyridoxal 5'-phosphate.
Pyridoxal 5'-phosphate (pyridoxal-5'-P) has been found to act as a bifunctional reagent during the inactivation of porcine heart cytoplasmic malate dehydrogenase (L-malate: NAD+ oxidoreductase, EC 1.1.1.37). The biphasic kinetics and X-azolidine-like structure formed were similar to those observed for mitochondrial malate dehydrogenase (Wimmer, M.J., Mo, T., Sawyers, D.L., and Harrison, J.H. (1...
متن کاملChemical modification of the avian progesterone receptor by pyridoxal 5'-phosphate.
Pyridoxal BP-phosphate inhibits the binding of the avian progesterone receptor to ATP-Sepharose, probably through a Schiff base interaction. It also blocks other interactions characteristic of the activated or transformed receptor, such as its binding to nuclei, DNA-cellulose, and phosphocellulose. In an attempt to explain these inhibitory effects, we have characterized the progesterone recepto...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1984
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.48.349