AFFINITY CHROMATOGRAPHY OF TYROSINE TRANSFER-RNAS

被引：7

作者：

GARCIA, CM ^{[1
]}

SINGHAL, RP ^{[1
]}

机构：

[1] WICHITA STATE UNIV,DEPT CHEM,WICHITA,KS 67208

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 86卷 / 03期

关键词：

D O I：

10.1016/0006-291X(79)91769-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Ricinus communis agglutinin, a lectin from castor beans has an affinity for β-d-galactose and tyrosine tRNAs of mammalian tissues have galactose in gal-Q base of their anticodons. We have studied interaction between tyrosine tRNAs and this lectin immobilized on solid supports using spacer arms of different lengths. Tyrosine tRNAs are separated from nineteen other tRNAs of bovine liver by affinity chromatography using the lectin immobilized to an agarose matrix. The results indicate that a spacer arm length of 10 Å between the agarose bead and the lectin gives the best separation. Two tyrosine tRNA isoacceptors are separated from each other and from other tRNAs in one step using this affinity column chromatography. © 1979.

引用

页码：697 / 703

页数：7

共 9 条

[1]

BRISCOE WT, 1975, CANCER RES, V35, P2586

[2]

Deutscher M P, 1974, Methods Enzymol, V29, P577

[3] STRUCTURE OF QSTAR NUCLEOSIDE ISOLATED FROM RABBIT LIVER TRANSFER RIBONUCLEIC-ACID [J].