NDLI: Crystalline L-ribulose 5-phosphate 4-epimerase from Escherichia coli.

Content Provider	Semantic Scholar
Author	Patrick, James Warner Masson, Maryline
Copyright Year	1968
Abstract	Abstract l-Ribulose 5-phosphate 4-epimerase has been crystallized from l-arabinose-induced cells of Escherichia coli B/r strain F' araB-24/araB-24 after a 40-fold purification. The enzyme is homogeneous in the ultracentrifuge and 98% pure by acrylamide gel disc electrophoresis. The molecular weight determined by sedimentation equilibrium is 1.03 ± 0.01 x 105. The enzyme is free of d-ribulose 5-phosphate 3-epimerase activity, does not exhibit any cofactor requirement, and shows maximal activity from pH 7 to 10. An amino acid analysis is presented.
File Format	PDF HTM / HTML
PubMed reference number	4879898
Journal	Medline
Volume Number	243
Issue Number	18
Alternate Webpage(s)	http://www.jbc.org/content/243/18/4700.full.pdf
Journal	The Journal of biological chemistry
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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