Abstract
Two starch gel electrophoretic variants of glucose 6-phosphate dehydrogenase (G6PD) in Drosophila melanogasterwere partially purified and characterized biochemically. The difference in their migration on starch gel is not due to a charge difference, but rather to a difference in molecular size due to instability of one of the variants. Crosses between the two variants did not produce offspring showing an intermediate electrophoretic band in the heterozygous female. That an hybrid molecule does exist in the heterozygous female, however, was demonstrated by taking advantage of differences in heat lability and structural stability of the two variants. Hence, we conclude that the G6PD locus in both X-chromosomes is active in each cell in female Drosophila.Our findings with DrosophilaG6PD emphasize the importance to protein variation and enzyme function of mutations leading to amino acid substitutions which do not produce a change in net charge.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
