Electronic Resource
Oxford, UK
:
Blackwell Publishing Ltd
FEMS microbiology letters
29 (1985), S. 0
ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
Abstract 1-Phosphofructokinase has been purified from Escherichia coli. Size exclusion chromatography revealed an Mr of 57000. After sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE) we found a single protein band corresponding to an Mr of 30000. The enzyme was highly specific for fructose-1-phosphate. ATP and GTP were the best phosphoryl donors, whereas UTP and CTP showed only a weak effect. The enzyme was reversibly inhibited by fructose-1, 6-bisphosphate and ADP and irreversibly by phenyl-methanesulfonyl fluoride (PMSF). ATP prevented irreversible inhibition by PMSF. Fructose-1-phosphate had a much less pronounced effect on irreversible inhibition by PMSF. Comparison of the peptide map of tryptic digested 1-phosphofructokinase and PMSF-modified 1-phosphofructokinase revealed an additional peak for the modified 1-phosphofructokinase whereas the intensity of another peak was lowered compared to untreated 1-phosphofructokinase. This peptide might therefore represent the binding site for ATP.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1574-6968.1985.tb00868.x
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