ISSN:
1573-4927
Keywords:
Drosophila melanogaster
;
phosphoglucomutase
;
polymorphism
;
enzyme kinetics
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract Phosphoglucomutase (PGM) of adult stage in Drosophila melanogaster has been characterized by gel filtration, ion-exchange chromatography, and isoelectric focusing. The two common electrophoretic variants, PGMA and PGMB, differ with respect to their kinetic and stability parameters. PGMA is more thermostable than PGMB but shows the same pH optimum, equal dependence on Mg2+, and identical molecular weight. There is no significant kinetic difference between the two allozymes at the optimum pH value, but at pH 6.0 the K m value for glucose-1,6-diphosphate of PGMB is significantly higher than that of PGMA. This difference might explain the observed selective advantage of the Pgm A allele in population studies.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00504306
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