NDLI: Reversal of UDP-galactose 4-epimerase deficiency of human leukocytes in culture.

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Reversal of UDP-galactose 4-epimerase deficiency of human leukocytes in culture.

Content Provider	Semantic Scholar
Author	Mitchell, B. Egan Steinmann, Beat Gitzelmann, Richard
Copyright Year	1975
Abstract	Stimulation with phytohemagglutinin of the leukocytes from six of the seven known individuals with UDP-galactose 4-epimerase (= UDP-glucose 4-epimerase; EC 5.1.3.2) deficiency consistently resulted in the appearance of epimerase activity in the cultured cells. A long-term lymphoblast culture derived from one proband also contained an active epimerase enzyme. A comparison of the properties of this enzyme with those of epimerase produced by control lymphoblast lines revealed comparable Km values for UDP-galactose and NAD and identical behavior on polyacrylamide electrophoresis. However, a difference in the NAD requirement for heat stability at 40 degree provided some evidence for a structural defect in this enzyme. Possible explanations for the appearance of UDP-galactose 4-epimerase activity in stimulated lymphocytes include an increased rate of synthesis of a mutant enzyme and a derepression of an epimerase locus during lymphocyte transformation.
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.pnas.org/content/72/12/5026.full.pdf
PubMed reference number	1748v1
Volume Number	72
Issue Number	12
Journal	Proceedings of the National Academy of Sciences of the United States of America
Language	English
Access Restriction	Open
Subject Keyword	Contain (action) Dysplastic Nevus Electrophoresis Epimerases Galactose Glucose Lymphocyte Activation Proband (finding) UDP-glucose 4-epimerase activity UDPglucose 4-epimerase deficiency disease Uridine Diphosphate explanation lymphoblast polyacrylamide
Content Type	Text
Resource Type	Article

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