QUATERNARY STRUCTURE OF LACTATE DEHYDROGENASE .I. SUBUNIT MOLECULAR WEIGHT AND REVERSIBLE ASSOCIATION AT ACID PH

被引：26

作者：

MILLAR, DB

FRATTALI, V

WILLICK, GE

机构：

[1] Laboratory of Physical Biochemistry, Naval Medical Research Institute, National Naval Medical Center, Bethesda

[2] National Academy of Sciences-National Research Council, Naval Medical Research Institute

来源：

BIOCHEMISTRY | 1969年 / 8卷 / 06期

关键词：

D O I：

10.1021/bi00834a025

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 monomer subunit molecular weight of lactate dehydrogenase has been shown to be 18,000 by sedimentation equilibrium studies in 6.2 m guanidine hydrochloride at pH 2. It was demonstrated that 7 m guanidine hydrochloride at pH 7 was not sufficient to complete the dissociation. Lactate dehydrogenase undergoes a reversible association at pH 2. The association was analyzed in terms of a model containing monomers, dimers, tetramers, and octamers in equilibrium. A monomer molecular weight of 18,000, when coupled with an amino acid analysis, indicates lactate dehydrogenase must contain at least two nonidentical chains. Application of the above analysis to two restricted cases with two nonidentical chains is discussed. © 1969, American Chemical Society. All rights reserved.

引用

页码：2416 / &

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