Abstract
A rapid and efficient procedure has been developed for the purification of α‐glycerophosphate dehydrogenase from the tephritid fly Anastrepha suspensa. This procedure is applicable to the isolation of the enzyme from other tephritids. The A. suspensa α‐glycerophosphate dehydrogenase is dimeric with a molecular weight of 70,000 and a subunit molecular weight of 35,000. The pH optimum of the enzyme is 7.0. The amino acid composition is compared with that of other α‐glycerophosphate dehydrogenases. By means of the quantitative microcomplement fixation procedure the A. suspensa α‐glycerophosphate dehydrogenase is compared immunologically to a variety of other tephritid and dipteran α‐glycerophosphate dehydrogenases.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 271-286 |
| Number of pages | 16 |
| Journal | Archives of Insect Biochemistry and Physiology |
| Volume | 4 |
| Issue number | 4 |
| DOIs | |
| State | Published - Apr 1987 |
Keywords
- biochemical studies
- immunological studies
- tephritid
ASJC Scopus subject areas
- Physiology
- Biochemistry
- Insect Science