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- W2285703679 abstract "The alternate procedures used in the tyrosine apodecarboxylase assays for pyridoxal 5'-phosphate were evaluated to determine optimal conditions. Two preparations of tyrosine apodecarboxylase from S. faecalis were used: a cell suspension and a partially purified cell-free form. The activity of the decarboxylase was measured in two different assays using (/sup 14/C)tyrosine or (/sup 3/H)tyrosine as substrate. The presence of serum proteins inhibited both assays for serum pyridoxal-P; since a higher concentration of serum was used in the (/sup 14/C)-tyrosine assay, that assay was inhibited to a greater extent. In contrast, addition of deproteinized serum extract did not appear to inhibit either assay. The rate of reconstitution of the apodecarboxylase in the cell suspension was at least four times slower than that of the cell-free enzyme. The rate of reconstitution of the cell-free enzyme was faster in acetate than in citrate buffer. Inorganic sulfate or phosphate, at normal plasma concentrations, did not alter either the reconstitution rate of tyrosine decarboxylase or the final activity obtained in the assays using either substrate. The tyrosine apodecarboxylase assay for pyridoxal-P can be optimized by using deproteinized sera or plasma and incubating the cell-free apoenzyme with the coenzyme in acetate buffer for sufficient time tomore » obtain maximum reconstitution.« less" @default.
- W2285703679 created "2016-06-24" @default.
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- W2285703679 date "1986-05-01" @default.
- W2285703679 modified "2023-09-23" @default.
- W2285703679 title "Evaluations of tyrosine apodecarboxylase assays for pyridoxal phosphate" @default.
- W2285703679 hasPublicationYear "1986" @default.
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