Chemical modification of the avian progesterone receptor by pyridoxal 5'-phosphate.

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Chemical 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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Binding 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...

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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 ...

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Reversible modification of pig heart mitochondrial malate dehydrogenase by pyridoxal 5'-phosphate.

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Transfer of pyridoxal 5'-phosphate from albumin-pyridoxal 5'-phosphate complex to apo-aspartate aminotransferase.

Pyridoxal 5•L-phosphate (PLP) is known to combine with bovine serum albumin to form a(1:1) complex which scarcely dissociates, even when subjected to intensive dialysis. When this complex was incubated with apo-aspartate aminotransferase (apoGOT) for an appropriate time and the preincubated mixture then submitted to the usual GOT assay, the appearance of GOT activity was obviously confirmed, in...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1979

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)86824-2