Pyridoxal-5′-phosphate as a probe for rotational diffusion
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چکیده
منابع مشابه
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 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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Pyridoxal phosphate-dependent histidine decarboxylase from Morganella morganii AM-15 was inactivated by (a-a-fluoromethylhistidine by a pseudo firstorder reaction, with KI and kinact values of 0 . 1 mM and 32.2 min-l, respectively, and was most efficient at pH 6.5-7.0. Both L-histidine and the competitive inhibitor, L-histidine methyl ester, protected against inactivation. The apoenzyme was not...
متن کاملBiomedical aspects of pyridoxal 5'-phosphate availability.
The biologically active form of vitamin B6, pyridoxal 5'-phosphate (PLP), is a cofactor in over 160 enzyme activities involved in a number of metabolic pathways, including neurotransmitter synthesis and degradation. In humans, PLP is recycled from food and from degraded PLP-dependent enzymes in a salvage pathway requiring the action of pyridoxal kinase, pyridoxine 5'-phosphate oxidase and phosp...
متن کاملAspartate transcarbamylase from Escherichia coli. The use of pyridoxal 5'-phosphate as a probe in the active site.
Spectrophotometric titration studies at pH 8.0 have revealed that pyridoxal 5’-phosphate binds as a Schiff base to the catalytic subunit of Escherichia coli aspartate transcarbamylase with a stoichiometry of 3 pyridoxal phosphates per trimer and a dissociation constant of 0.9 pM. The ultraviolet absorption of the Schiff base near 430 nm is lost upon addition of the inhibitor N-(phosphonacetyl)-...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1983
ISSN: 0014-5793
DOI: 10.1016/0014-5793(83)80186-0