Stabrovskaia V I, Braun A D
Biofizika. 1982 May-Jun;27(3):371-4.
Stability of lactatedehydrogenase (LDG) and glucose-6-phosphate dehydrogenase (G-6-PhDG) to the action of heating and urea on the muscle and on the enzymes isolated from muscle was studied. By the stability to the thermal agent in the system of the muscle and out of it LDG and G-6-PhDG exceed creatine kinase and aldolase; the most thermostable enzyme is G-6-PhDG. According to the action of urea on the muscle G-6-PhDG is the most stable enzyme, LDG is the most labile one among the studied enzymes. Under the action of urea on the isolated enzymes G-6-PhDG is the most labile one.
研究了乳酸脱氢酶（LDG）和葡萄糖-6-磷酸脱氢酶（G-6-PhDG）在肌肉以及从肌肉中分离出的酶中对加热和尿素作用的稳定性。就肌肉系统内外对热剂的稳定性而言，LDG和G-6-PhDG超过肌酸激酶和醛缩酶；最耐热的酶是G-6-PhDG。根据尿素对肌肉的作用，G-6-PhDG是最稳定的酶，而LDG是所研究酶中最不稳定的一种。在尿素对分离出的酶的作用下，G-6-PhDG是最不稳定的一种。
