Purification and cDNA cloning of the alcohol dehydrogenase of the flesh fly Sarcophaga peregrina. A structural relationship between alcohol dehydrogenase and a 25-kDa protein.
We purified to homogeneity two proteins with molecular masses of 25 kDa from the fat body of the Sarcophaga larva. One was alcohol dehydrogenase (ADH) and the other was a 25-kDa protein of which the genomic DNA had been cloned. We isolated the cDNA for ADH and determined its amino acid sequence. Amino acid sequence identity between ADH and the 25-kDa protein was 40%, indicating that they are structurally related proteins. The amount of ADH in Sarcophaga was almost constant through the larval stage to the adult stage, but the 25-kDa protein was detected only within a restricted period between the final larval instar and the early pupal stage.
Horio
T
T
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Kubo
T
T
Natori
S
S
D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics*; D004175:Diptera / Q000201:enzymology* / Q000235:genetics* / Q000254:growth & development; D005216:Fat Body / Q000201:enzymology; D018507:Gene Expression Regulation, Developmental; D015971:Gene Expression Regulation, Enzymologic; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D011506:Proteins; D000426:Alcohol Dehydrogenase