Biology Faculty Articles

Title

Comparative Analysis of Malate Dehydrogenases of Drosophila melanogaster

Document Type

Article

Publication Date

10-1973

Publication Title

Biochemical Genetics

ISSN

0006-2928

Volume

10

Issue/No.

2

First Page

191

Last Page

205

Abstract

The malate dehydrogenases of D. melanogaster have been resolved into a cytoplasmic form (cMDH) and a mitochondrial matrix form (mMDH). Flies homozygous for allozyme variants exhibit isozymes of cMDH detected by starch gel electrophoresis and acrylamide gel isoelectric focusing. The basis of these isozymes was investigated, and the results suggest either conformational or epigenetic modification of isozymes. The probable structural gene for cMDH (Mdh-1) has been mapped genetically by allozyme variants to II-35 ± 3 and cytologically by monitoring gene dosage in segmental aneuploids to between 28D and 29F on II-L of the Drosophila salivary gland chromosome map. The structural gene for mMDH is neither identical to nor in the near chromosomal proximity of Mdh-1. Nevertheless, the two enzymes exhibit markedly similar properties with respect to (1) catalytic activity, (2) pH optima, (3) pH optimum shift in response to different ionic environments, and (4) molecular weight as determined by sucrose density gradient sedimentation.

Comments

©1973 Kluwer Academic Publishers-Plenum Publishers

Additional Comments

National Institute of General Medical Sciences fellowship #: 6-FO2-GM-49, 633-01

ORCID ID

0000-0001-7353-8301

ResearcherID

N-1726-2015

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