Reddy A R, Pelliccia J G, Sofer W
Biochem Genet. 1980 Apr;18(3-4):339-51. doi: 10.1007/BF00484247.
Adhnll is an ethyl methanesulfonate induced mutant that lacks detectable alcohol dehydrogenase activity. A number of indirect lines of evidence have indicated that the mutation responsible for this loss in enzyme activity is localized in the Adh structural gene. We present more direct evidence for this hypothesis here. Utilizing a newly developed procedure for comparing tryptic peptides of Drosophila alcohol dehydrogenase obtained from different strains, we show that the alcohol dehydrogenase-like protein isolated from Adhnll exhibits an altered peptide profile when compared to that of wild type. The implications of this finding as well as the utility of the method for attacking other genetic and developmental problems are discussed.
Adhnll是一种由甲基磺酸乙酯诱导产生的突变体，缺乏可检测到的乙醇脱氢酶活性。许多间接证据表明，导致这种酶活性丧失的突变位于Adh结构基因中。我们在此为这一假说提供了更直接的证据。利用一种新开发的程序来比较从不同菌株获得的果蝇乙醇脱氢酶的胰蛋白酶肽段，我们发现，与野生型相比，从Adhnll中分离出的乙醇脱氢酶样蛋白呈现出改变的肽段图谱。本文讨论了这一发现的意义以及该方法在解决其他遗传和发育问题方面的实用性。
