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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.

Authors

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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.
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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 -