Increased Activity of Serum Aspartate Aminotransferase in the Presence of Added Pyridoxal-5'-Phosphate
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چکیده
منابع مشابه
Increased aspartate aminotransferase activity of serum after in vitro supplementation with pyridoxal phosphate.
We examined the effect of pyridoxal phosphate supplementation on the apparent aspartate aminotransferase (EC 2.6.1.1.) activity of human serum. Supplementation by 25 mol/liter effected an average increase of 16% in the results for kinetic assay. The increase was not the result of increased enzymatic or nonenzymatic blanks, and, within a small range, sample dilution had no significant effect. Pa...
متن کاملTransfer 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...
متن کاملAspartate aminotransferase activity in human serum. Factors to be considered in supplementation with pyridoxal 5'-phosphate in vitro.
The pyridoxal phosphate reactivation of the apo form of aspartate aminotransferase (EC 2.6.1.1) in human serum has been studied with "normal" and above-normal activity of this enzyme. The extent of the reactionation did not depend on the presence of the substrates, L-aspartate or 2-oxoglutarate. Reactivation was greatest with 110 mumol of added pyridoxal phsophate present per liter during a pre...
متن کاملThe binding of pyridoxal 5-phosphate to aspartate aminotransferase of pig heart.
1. Oestrone 3-glucuronide has been identified as the reaction product after incubation of oestrone with a rabbit-liver microsomal preparation, uridine diphosphate glucuronic acid being used as the glucuronic acid donor. The formation of this compound was studied under various experimental conditions. 2. The reaction showed a maximum at pH 8.08-2, and Km for oestrone was found to be 9-7 x 10-5M....
متن کاملEffects of buffers on aspartate aminotransferase activity and association of the enzyme with pyridoxal phosphate.
Using purified enzymes of human origin and patients' sera, we examined factors influencing the in vitro association of pyridoxal phosphate with aspartate aminotransferase (EC 2.6.1.1). The rate of association was markedly retarded by phosphate buffer in comparison with tris(hydroxymethyl)aminomethane or six other buffers. Pyridoxal phosphate at an incubation concentration of 130 mumol/liter rea...
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ژورنال
عنوان ژورنال: Clinical Chemistry
سال: 1973
ISSN: 0009-9147,1530-8561
DOI: 10.1093/clinchem/19.1.140a