Yeast uridine diphosphogalactose-4-epimerase, correlation between activity and fluorescence

Yeast grown on galactose contains a strikingly fluorescent protein in the fractions which contain UDP-galactose-4-epimerase. UDP-galactose-4-epimerase from yeast, unlike the corresponding enzyme from liver, does not require addition of diphosphopyridine nucleotide for activity. Further purification...

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Bibliographic Details
Published inArchives of biochemistry and biophysics Vol. 78; no. 2; pp. 407 - 415
Main Authors Maxwell, Elizabeth S., de Robichon-Szulmajster, Huguette, Kalckar, Herman M.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.12.1958
Subjects
Fluorescence
Isomerases
Old Medline
Saccharomyces cerevisiae
UDPglucose 4-Epimerase
Uridine Diphosphate Galactose
Yeasts
FLUORESCENCE
ISOMERASES
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Summary:Yeast grown on galactose contains a strikingly fluorescent protein in the fractions which contain UDP-galactose-4-epimerase. UDP-galactose-4-epimerase from yeast, unlike the corresponding enzyme from liver, does not require addition of diphosphopyridine nucleotide for activity. Further purification for the yeast enzyme gives a close correlation between enzyme activity and fluorescence. Addition of p-chloromercuribenzoate brings about a disappearance of fluorescence as well as activity. The latter can be restored by addition of diphosphopyridine nucleotide. A discussion of possible mechanisms of the enzymic interconversion poses a number of new problems.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(58)90366-7