Drapeau G R
J Biol Chem. 1980 Feb 10;255(3):839-40.
Previous studies have described the isolation of mutationally altered proteases in Pseudomonas fragi (Noreau, J., and Drapeau, G.R. (1979) J. Bacteriol, 140, 911-916. In the present study, it is shown that one of these proteases cleaves specifically the peptide bonds on the NH2-terminal side of either aspartic acid or cysteic acid residues in oxidized ribonuclease. With myoglobin as the substrate, a similar specificity was observed except that only four out of the six aspartyl bonds present were hydrolyzed.
以往的研究已经描述了在脆弱拟杆菌中分离出突变的蛋白酶（诺罗，J.，和德拉波，G.R.（1979年）《细菌学杂志》，140，911 - 916）。在本研究中，表明这些蛋白酶之一特异性切割氧化核糖核酸酶中天冬氨酸或半胱氨酸残基的NH2 - 末端侧的肽键。以肌红蛋白为底物时，观察到类似的特异性，只是存在的六个天冬氨酰键中只有四个被水解。
