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乙酰亚氨酸甲酯的性质及其作为蛋白质修饰试剂的用途。

Properties of methyl acetimidate and its use as a protein-modifying reagent.

作者信息

Makoff A J, Malcolm A D

出版信息

Biochem J. 1981 Jan 1;193(1):245-9. doi: 10.1042/bj1930245.

DOI:10.1042/bj1930245
PMID:7305926
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1162596/
Abstract

The rate of hydrolysis of the imido ester methyl acetimidate and its rate of amidination of denatured aldolase were investigated under different conditions of temperature, pH and ionic strength. Both rate constants increase greatly with temperature, whereas ionic strength has no effect on either. The effect of pH is more complex. Between pH 6.8 and 8.8 the rate of hydrolysis decreases and the rate of amidination increases. These results are discussed in terms of the reaction mechanisms involved.

摘要

在不同温度、pH值和离子强度条件下,研究了亚氨酯甲基乙酰亚胺的水解速率及其对变性醛缩酶的脒化速率。两个速率常数均随温度大幅增加,而离子强度对两者均无影响。pH值的影响更为复杂。在pH 6.8至8.8之间,水解速率降低,脒化速率增加。根据所涉及的反应机理对这些结果进行了讨论。

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本文引用的文献

1
Identification of a class of lysines within the non-specific DNA-binding site of RNA polymerase core enzyme from Escherichia coli.大肠杆菌RNA聚合酶核心酶非特异性DNA结合位点内一类赖氨酸的鉴定。
Eur J Biochem. 1980 May;106(1):313-20. doi: 10.1111/j.1432-1033.1980.tb06025.x.
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Methods for obtaining peptide maps of proteins on a subnanomole scale.
Anal Biochem. 1975 Sep;68(1):175-84. doi: 10.1016/0003-2697(75)90692-2.
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Formation of non-amidine products in the chemical modification of horse liver alcohol dehydrogenase with imido esters.用亚胺酯对马肝醇脱氢酶进行化学修饰时非脒产物的形成。
Biochem Biophys Res Commun. 1975 Nov 3;67(1):133-8. doi: 10.1016/0006-291x(75)90293-4.
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Formation of non-amidine products in the reaction of primary amines with imido esters.
Biochem Biophys Res Commun. 1975 Nov 3;67(1):126-32. doi: 10.1016/0006-291x(75)90292-2.