Genetic and physiochemical studies on ?-hydroxy acid dehydrogenase in Anopheles albimanus

Abstract
β-Hydroxy acid dehydrogenase (β-Had-2) of Anopheles albimanus was assigned to chromosome 3. The apparent sequence of loci on chromosome 3 is hexokinase-1-22-stripe-28-β-hydroxy acid dehydrogenase-2-4-aldehyde oxidase-2-esterase-8-4-esterase-4-?-phosphoglucomutase-?-esterase-6. β-Hydroxy acid dehydrogenase is 25 and 30 map units from phosphoglucomutase and esterase-6, respectively. The one-band electromorph of β-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 β-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.