Reexamination of alcohol dehydrogenase structural mutants in Drosophila using protein blotting
Using protein blotting and an immuno-overlay procedure, the authors have reexamined the cross-reacting material produced by ADH null-activity mutants generated with ethyl methanesulfonate (EMS). Of the 13 mutants, 11 have an immunodetectable polypeptide of wild-type size. The native and urea denatured isoelectric points (pI) establish that 7 of 13 of the mutations have no effect on protein charge. The electrophoretic mobilities of each variant on increasing percent acrylamide gels (Ferguson analysis), reveal that 9 of the 11 immunodetectable mutations have retained the ability form dimers under native conditions. None of the inactive mutant proteins has the ability to form the adduct-bound isozyme. The authors have found no correlation between protein pI and i vivo stability. The observed frequencies of specific charge class alterations do not dispute the propensity of G:A transitions previously found for EMS mutagenesis.
- Research Organization:
- Univ. of Pennsylvania, Philadelphia
- OSTI ID:
- 5898252
- Journal Information:
- Genetics; (United States), Vol. 116:2
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
EMS
GENETIC EFFECTS
HEMIACETAL DEHYDROGENASES
MUTANTS
BIOCHEMISTRY
DROSOPHILA
ELECTROPHORESIS
ENZYME ACTIVITY
PROTEINS
ANIMALS
ARTHROPODS
BIOLOGICAL EFFECTS
CHEMISTRY
DIPTERA
ENZYMES
ESTERS
FLIES
FRUIT FLIES
INSECTS
INVERTEBRATES
MUTAGENS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
OXIDOREDUCTASES
SULFONIC ACID ESTERS
560300* - Chemicals Metabolism & Toxicology
550400 - Genetics