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TISSUE-SPECIFIC GLUCOSE 6-PHOSPHATE DEHYDROGENASES IN ANOPHELINE MOSQUITOES

UMBERTO BIANCHI 1 and ANTONIETTINA RINALDI 1

1 Institute of Genetics, University of Cagliari, Cagliari, Italy

Glucose 6-phosphate dehydrogenase (G6PD) electrophoretic variants have been detected in single adult homogenates by screening laboratory strains of Anopheles atroparvus, Anopheles labranchiae and Anopheles stephensi. Pair mating crosses of A. atroparvus individuals set up to study the inheritance mechanism of this apparent polymorphism failed to show Mendelian segregation. Furthermore, monomorphic and tissue-specific G6PD bands were obtained from single adult "midgut" and single adult "skin" homogenates and the apparent polymorphism disappeared. However, the electrophoretic heterogeneity reappeared when 10 µl of the gut homogenate were added to an equal volume of the skin homogenate and permitted to interact in vitro at room temperature (20-25°C) for 4-5 min. Bovine trypsin greatly modified the anodical mobility of the skin isoenzyme. Single whole homogenates, prepared in buffers containing soybean (trypsin inhibitor), partially retained the electrophoretic heterogeneity. On this experimental background it is possible to draw the following conclusions: (a) at least two monomorphic and tissue-specific (gut and skin) G6PD isoenzymes are present in the anopheline species studied by us; (b) a factor (or factors) possessing a trypsin-like action seems to be present in the whole body homogenate, this factor seems to be particularly active in interacting with the skin enzyme; and (c) the occurrence of a similar interaction could facilitate the formation of G6PD catalytically active molecular artifacts. These data and analogous results obtained by other authors permitted us to conclude that if genetic analysis has not been performed it is very hazardous to interpret zymograms simply by assuming that any electrophoretic heterogeneity necessarily represents a genetic polymorphism.

Submitted on August 17, 1973


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