磷脂脂质体相互作用可抑制牛肌肉和心脏乳酸脱氢酶的有限蛋白水解。
Limited proteolysis of bovine muscle and heart lactate dehydrogenase is inhibited by phospholipid liposome interaction.
作者信息
Dabrowska A, Czapińska E
机构信息
Department of Biochemistry, Academy of Medicine, Wrocław, Poland.
出版信息
Biochim Biophys Acta. 1990 Sep 7;1027(3):301-3. doi: 10.1016/0005-2736(90)90322-f.
Limited proteolysis of phospholipid complexes of heart and muscle bovine lactate dehydrogenase by trypsin and chymotrypsin has been studied under nondenaturing condition at pH 7.5. Chymotrypsin cleaves the polypeptide chain of heart and muscle lactate dehydrogenase into two principal fragments and LDH subunits were protected by lipids towards the proteinase attack. Enzymatic activity of heart and muscle lactate dehydrogenase was abolished by limited proteolytic cleavage. In complexes, both isoenzymes were protected against proteinases attack by lipids.
在pH 7.5的非变性条件下，研究了胰蛋白酶和胰凝乳蛋白酶对牛心脏和肌肉乳酸脱氢酶磷脂复合物的有限蛋白水解作用。胰凝乳蛋白酶将心脏和肌肉乳酸脱氢酶的多肽链切割成两个主要片段，并且乳酸脱氢酶亚基受到脂质的保护而免受蛋白酶攻击。心脏和肌肉乳酸脱氢酶的酶活性通过有限的蛋白水解切割而被消除。在复合物中，两种同工酶都受到脂质的保护而免受蛋白酶攻击。
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