| Autor: |
Eisses, Karel Th., Davies, Suzanne L., Chambers, Geoffrey K. |
| Zdroj: |
Biochemical Genetics; April 1994, Vol. 32 Issue: 3-4 p91-103, 13p |
| Abstrakt: |
Purified thermostable alcohol dehydrogenase allozymes ADH-71k and ADH-FCh.D. ofDrosophila melanogaster have been compared with the two common enzyme forms ADH-F and ADH-S. Enzyme kinetic parameters for various primary and secondary alcohols were determined under standard conditions used previously. Both ADH-71k and ADH-FCh.D. show ADH-S-like reaction kinetics andKm values, due to retrograde evolution at site 214, Pro ? Ser. Inhibition studies with alcohol dehydrogenase inhibitors pyrazole, 4-methylpyrazole, and cibacron blue 3GA were also performed. Activity measurements on crude extracts of larvae and flies from isogenic lines of ADH-FCh.D. revealed a consistently higher activity than in ADH-71k-containing strains, in contrast to the original strains. |
| Databáze: |
Supplemental Index |
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