大肠杆菌核糖体对变性乳酸脱氢酶的重折叠作用
Refolding of denatured lactate dehydrogenase by Escherichia coli ribosomes.
作者信息
Chattopadhyay S, Das B, Bera A K, Dasgupta D, Dasgupta C
机构信息
Department of Biophysics, Molecular Biology and Genetics, University of Calcutta, India.
出版信息
Biochem J. 1994 Jun 15;300 ( Pt 3)(Pt 3):717-21. doi: 10.1042/bj3000717.
Abstract
Escherichia coli ribosomes were used to refold denatured lactate dehydrogenase from porcine muscle. This activity of ribosomes, unlike most of the chaperons, did not require the presence of ATP. The molar concentration of ribosomes required for this refolding was comparable with that of the enzyme. Restoration of the enzyme activity was demonstrated using assays for both the forward and backward reactions. Binding of the denatured enzyme to ribosomes and its refolding were fairly rapid processes as revealed by the time course of the reaction and inhibition of folding when the denatured enzyme was allowed to refold spontaneously for short times before the addition of ribosomes. This protein-folding activity was detected in 70 S ribosomes as well as its RNA, in 50 S particles and in 23 S rRNA. However, 30 S particles failed to refold the enzyme.
摘要
使用大肠杆菌核糖体对猪肌肉中变性的乳酸脱氢酶进行复性。核糖体的这种活性与大多数伴侣蛋白不同，不需要ATP的存在。这种复性所需的核糖体摩尔浓度与酶的摩尔浓度相当。通过正向和反向反应的测定证明了酶活性的恢复。变性酶与核糖体的结合及其复性是相当快速的过程，这从反应的时间进程以及在加入核糖体之前让变性酶短时间自发复性时折叠受到抑制可以看出。在70S核糖体及其RNA、50S颗粒和23S rRNA中都检测到了这种蛋白质折叠活性。然而，30S颗粒无法使该酶复性。
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