变性兔肌肉肌酸激酶的重折叠。探寻重折叠过程中的中间体以及活性巯基修饰对重折叠的影响。
The refolding of denatured rabbit muscle creatine kinase. Search for intermediates in the refolding process and effect of modification at the reactive thiol group on refolding.
作者信息
Price N C, Stevens E
出版信息
Biochem J. 1982 Jan 1;201(1):171-7. doi: 10.1042/bj2010171.
Abstract
A number of aspects of the refolding of denatured rabbit muscle creatine kinase have been studied. Addition of substrates has no effect on the rate or extent of regain of activity. The changes in protein fluorescence during refolding broadly parallel the regain of activity. A study of the susceptibility of the enzyme to proteolysis during refolding indicates that there is no significant accumulation of folded, but inactive, intermediates in the folding process. Modification of the reactive thiol group on each subunit of the enzyme by small reagents such as iodoacetate or iodoacetamide prior to denaturation has only a small effect on the rate of subsequent refolding. However, modification by the bulky reagent 6-(4-iodoacetamidophenyl)aminonaphthalene-2-sulphonate has a very large effect on the ability of the enzyme to refold after denaturation.
摘要
已对变性兔肌肉肌酸激酶复性的多个方面进行了研究。添加底物对活性恢复的速率或程度没有影响。复性过程中蛋白质荧光的变化与活性恢复大致平行。对复性过程中酶对蛋白水解敏感性的研究表明，在折叠过程中没有明显积累已折叠但无活性的中间体。在变性前用碘乙酸盐或碘乙酰胺等小分子试剂修饰酶每个亚基上的反应性巯基，对随后的复性速率只有很小的影响。然而，用大分子试剂6-(4-碘乙酰氨基苯基)氨基萘-2-磺酸盐进行修饰，对变性后酶的复性能力有非常大的影响。
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本文引用的文献
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Biochim Biophys Acta. 1980 Feb 27;621(2):305-14. doi: 10.1016/0005-2795(80)90182-8.
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Inhibition of adenosine 5'-triphosphate-creatine phosphotransferase by substrate-anion complexes. Evidence for the transition-state organization of the catalytic site.底物 - 阴离子复合物对腺苷5'-三磷酸 - 肌酸磷酸转移酶的抑制作用。催化位点过渡态组织的证据。
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