HETEROGENEITY OF PRESUMABLY HOMOGENEOUS PROTEIN PREPARATIONS

被引：113

作者：

SUSOR, WA

KOCHMAN, M

RUTTER, WJ

机构：

[1] Departments of Biochemistry and Genetics, University of Washington, Seattle

[2] Department of Biochemistry and Biophysics, University of California Medical Center, San Francisco

[3] Department of Biochemistry, Medical School, Wroclaw

来源：

SCIENCE | 1969年 / 165卷 / 3899期

关键词：

D O I：

10.1126/science.165.3899.1260

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Some highly purified glycolytic enzymes have been subjected to isoelectric focusing and found to contain a number of enzymatically active species. Crystalline aldolase A and glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle were resolved into five components, crystalline aldolase from yeast was resolved into three components, pyruvate kinase from rabbit muscle yielded four components, and yeast enolase was resolved into two components. Rabbit muscle lactate dehydrogenase (M4) gave one major peak of protein and enzymatic activity. The profiles of aldolase, glyceraldehyde-3-phosphate dehydrogenase, and yeast aldolases suggest random combinations of two closely related subunits into tetramers and dimers, respectively. The molecular heterogeneity of the other enzymes is not so easily related to subunit structure.

引用

页码：1260 / &

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