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Studies on 3-Deoxy-D-flrafow0he.ptulosonate-7-phosphate Synthetase(phe) from Escherichia coli K12 1. Purification and Subunit Structure.

Authors :
Simpson, Richard J.
Davidson, Barrie E.
Source :
European Journal of Biochemistry; Nov76 Part 2, Vol. 70 Issue 2, p493-500, 8p
Publication Year :
1976

Abstract

1. 3-Deoxy-D-arabinoheptulosonate-7-phosphate synthetase(phe) from Escherichia coli K12 has been purified to near homogeneity. The purified enzyme has a specific activity of 67 units mg which is about 1000 times that found in cell-free extracts of wild-type E. coli K12. 2. The minimum molecular weight of the enzyme was estimated by dodecylsulphate-gel electrophoresis to be 33000. Re-estimation of the native molecular weight by gel filtration confirmed the previously determined value of 110000. 3. Amino acid analysis and tryptic fingerprints indicated that the subunits of the enzyme are very similar and possibly identical. 4. The purified enzyme does not contain Co<superscript>2+</superscript>. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00142956
Volume :
70
Issue :
2
Database :
Complementary Index
Journal :
European Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
20452908
Full Text :
https://doi.org/10.1111/j.1432-1033.1976.tb11040.x