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[Glucose-6-phosphate dehydrogenase of Drosophila melanogaster: purification and some properties of normal and mutant enzyme forms].
Biokhimiia. 1981 Mar; 46(3):542-51.B

Abstract

Two isozymes of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) (G6PD) of Drosophila melanogaster encoded by allelic genes were purified 3000-fold by biospecific phosphocellulose chromatography, using NADP as the enzyme eluent. Electrophoretically fast isozyme A and slow isozyme B variants prove to contain identical subunits with molecular weight of 54000-55000. G6PD is shown to be a dimer. An antiserum directed to highly purified isozyme A does not inhibit the activity of both isozymes. The mutant forms of G6PD restoring the viability of flies without 6-phosphogluconate dehydrogenase show drastically increased Km values for NADP and/or glucose-6-phosphate. It was demonstrated for two mutations that a sharp (200-fold) magnification of Km value for the substrate followed by a considerable increase in the enzyme thermostability might not exert any essential influence on the Km value for NADP.

Links

organism-specific

Authors

Kogan GL
No affiliation info available
Rozovskiĭ IaM
No affiliation info available
Gvozdev VA
No affiliation info available

MeSH

AllelesAnimalsDrosophila melanogasterGlucosephosphate DehydrogenaseImmune SeraImmunoassayIsoenzymesKineticsMacromolecular SubstancesMolecular WeightMutation

Pub Type(s)

Comparative Study
English Abstract
Journal Article

Language

rus

PubMed ID

6786379

Citation

Kogan, G L., et al. "[Glucose-6-phosphate Dehydrogenase of Drosophila Melanogaster: Purification and some Properties of Normal and Mutant Enzyme Forms]." Biokhimiia (Moscow, Russia), vol. 46, no. 3, 1981, pp. 542-51.
Kogan GL, Rozovskiĭ IaM, Gvozdev VA. [Glucose-6-phosphate dehydrogenase of Drosophila melanogaster: purification and some properties of normal and mutant enzyme forms]. Biokhimiia. 1981;46(3):542-51.
Kogan, G. L., Rozovskiĭ, I. a. M., & Gvozdev, V. A. (1981). [Glucose-6-phosphate dehydrogenase of Drosophila melanogaster: purification and some properties of normal and mutant enzyme forms]. Biokhimiia (Moscow, Russia), 46(3), 542-51.
Kogan GL, Rozovskiĭ IaM, Gvozdev VA. [Glucose-6-phosphate Dehydrogenase of Drosophila Melanogaster: Purification and some Properties of Normal and Mutant Enzyme Forms]. Biokhimiia. 1981;46(3):542-51. PubMed PMID: 6786379.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - [Glucose-6-phosphate dehydrogenase of Drosophila melanogaster: purification and some properties of normal and mutant enzyme forms]. AU - Kogan,G L, AU - Rozovskiĭ,Ia M, AU - Gvozdev,V A, PY - 1981/3/1/pubmed PY - 1981/3/1/medline PY - 1981/3/1/entrez SP - 542 EP - 51 JF - Biokhimiia (Moscow, Russia) JO - Biokhimiia VL - 46 IS - 3 N2 - Two isozymes of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) (G6PD) of Drosophila melanogaster encoded by allelic genes were purified 3000-fold by biospecific phosphocellulose chromatography, using NADP as the enzyme eluent. Electrophoretically fast isozyme A and slow isozyme B variants prove to contain identical subunits with molecular weight of 54000-55000. G6PD is shown to be a dimer. An antiserum directed to highly purified isozyme A does not inhibit the activity of both isozymes. The mutant forms of G6PD restoring the viability of flies without 6-phosphogluconate dehydrogenase show drastically increased Km values for NADP and/or glucose-6-phosphate. It was demonstrated for two mutations that a sharp (200-fold) magnification of Km value for the substrate followed by a considerable increase in the enzyme thermostability might not exert any essential influence on the Km value for NADP. SN - 0320-9725 UR - https://www.unboundmedicine.com/medline/citation/6786379/[Glucose_6_phosphate_dehydrogenase_of_Drosophila_melanogaster:_purification_and_some_properties_of_normal_and_mutant_enzyme_forms]_ L2 - http://flybase.org/cgi-bin/uniq.html?db=fbrf&field=pubmed_id&context=6786379 DB - PRIME DP - Unbound Medicine ER -