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来自面包酵母的苯丙氨酰-tRNA合成酶:tRNA亲和洗脱的特异性和定量分析

Phenylalanyl-tRNA synthetase from baker's yeast: specificity and quantitation of affinity elution with tRNA.

出版信息

Hoppe Seylers Z Physiol Chem. 1976 Jun;357(6):819-23. doi: 10.1515/bchm2.1976.357.1.819.

Abstract

TRNAPhe is able to elute phenylalanyl-tRNA synthetase from cation exchangers in a 1:1 ratio. Elution of phenylalanyl-tRNA synthetase in a 1:1 ratio is also observed for four noncognate tRNAs investigated, specific for valine, serine, isoleucine and tyrosine. If protein mixtures are subjected to affinity elution the cognate pair [tRNAPhe-phenylalanyl-tRNA synthetase] is eluted first, followed by noncognate pairs. The unspecific elution is not influenced by complexation of phenylalanyl-tRNA synthetase with an analog of phenylalanyl-adenylate.

摘要

tRNAPhe能够以1:1的比例从阳离子交换剂上洗脱苯丙氨酰-tRNA合成酶。对于所研究的四种非同源tRNA(分别特异于缬氨酸、丝氨酸、异亮氨酸和酪氨酸),也观察到以1:1的比例洗脱苯丙氨酰-tRNA合成酶。如果对蛋白质混合物进行亲和洗脱,同源对[tRNAPhe-苯丙氨酰-tRNA合成酶]首先被洗脱,随后是非同源对。非特异性洗脱不受苯丙氨酰-tRNA合成酶与苯丙氨酰-腺苷酸类似物络合的影响。

相似文献

3
Yeast phenylalanyl-tRNA synthetase: isolation of subunits on organomercurial-sepharose columns.
FEBS Lett. 1975 Apr 15;53(1):23-5. doi: 10.1016/0014-5793(75)80672-7.

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