Electronic Resource
Oxford, UK
:
Blackwell Publishing Ltd
Journal of neurochemistry
35 (1980), S. 0
ISSN:
1471-4159
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
The substrate activity of pyridoxamine (PM) for brain pyridoxal (PL) kinase was examined in view of a recent report which indicated that PM was a poor substrate for this enzyme. Bovine brain PL kinase was shown by liquid chromatography to catalyze the phosphorylation of PM (Km= 65 μm). The identity of the reaction product, pyridoxamine 5′-phosphate, was confirmed by its ability to act as a substrate for liver pyridoxine (pyridoxamine) 5′-phosphate oxidase. These results, which indicate that PM is a good substrate for brain PL kinase, are consistent with the proposed role of intracellular phosphorylation in the uptake of vitamin B-6 brain tissue.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1471-4159.1980.tb06297.x
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