REGULATION OF THYROID-HORMONE BINDING TO ITS CYTOSOLIC BINDING-PROTEIN BY L-ALPHA-ALANINE

被引：12

作者：

ASHIZAWA, K ^{[1
]}

KATO, H ^{[1
]}

MCPHIE, P ^{[1
]}

CHENG, SY ^{[1
]}

机构：

[1] NCI,BIOCHEM & METAB LAB,BETHESDA,MD 20892

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 167卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)92065-8

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：

The human cytosolic thyroid hormone binding protein (p58) was recently shown to be a monomer of pyruvate kinase, subtype PKM2, and have intrinsic pyruvate kinase activity. The present study evaluated the effect of L-α-alanine on the binding of 3,3′,5-triiodo-L-thyronine (T3) and enzymatic activity of p58. Analysis of the competitive binding data indicated that alanine, at the physiological concentration, is a non-competitive inhibitor of T3 binding to p58. Furthermore, alanine was found to be a "mixed" inhibitor of the substrate phosphoenol pyruvate. However, binding of alanine to p58 did not block the association of p58 to form the tetrameric pyruvate kinase. © 1990.

引用

页码：587 / 592

页数：6

共 11 条

[1] STRUCTURAL SIMILARITIES IN THE PLASMA-MEMBRANE 3,3',5-TRIIODO-L-THYRONINE RECEPTORS FROM HUMAN, RAT AND MOUSE CULTURED-CELLS - ANALYSIS BY AFFINITY LABELING [J].