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Genetic and physiochemical studies on β-hydroxy acid dehydrogenase inAnopheles albimanus

✍ Scribed by S. Narang; J. A. Seawright


Publisher
Springer
Year
1983
Tongue
English
Weight
422 KB
Volume
21
Category
Article
ISSN
0006-2928

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✦ Synopsis


beta-Hydroxy acid dehydrogenase (beta-Had-2) of Anopheles albimanus was assigned to chromosome 3. The apparent sequence of loci on chromosome 3 is hexokinase-1--22--stripe--28--beta-hydroxy acid dehydrogenase-2--4--aldehyde oxidase--2--esterase-8--4--esterase-4--?--phosphoglucomutase--?--esterase-6. beta-Hydroxy acid dehydrogenase is 25 and 30 map units from phosphoglucomutase and esterase-6, respectively. The one-band electromorph of beta-Had-2 in homozygotes and the three-band type in heterozygotes suggest that the enzyme is a dimer. A variety of electrophoretic techniques and spectrophotometric analysis were used to determine if the allozymes of beta-Had-2 can be differentiated on a basis other than mobility. No differences were detected among the allozymes on the basis of thermostability, urea denaturation, response to thiol reagents, chelating agents, or changes in coenzyme and substrate concentrations. No heterogeneity within allozymes separated by electrophoresis was detected by using thermostability tests.


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A mutant Hadnl was induced in Drosophila melanogaster and found to be deficient in beta-hydroxy acid dehydrogenase. This mutation was utilized to study the genetics and physiological expression of Had+ . Had+ was mapped to the X chromosome at 54.4 and seems to be the structural gene for the enzyme.