PURIFICATION AND PROPERTIES OF 2,3-DIPHOSPHOGLYCERIC ACID PHOSPHATASE FROM HUMAN ERYTHROCYTES

被引：32

作者：

HARKNESS, DR

ROTH, S

机构：

[1] Department of Medicine, University of Miami, Miami, FL

[2] Department of Biochemistry, University of Miami, Miami, FL

[3] Miami Veterans Administration Hospital, Miami, FL

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1969年 / 34卷 / 06期

关键词：

D O I：

10.1016/0006-291X(69)90258-7

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：

A 1200-fold purification of an enzyme from human erythrocytes which hydrolyzes 2,3-diphosphoglyceric acid (2, 3-DPG) to Pi and 3-phosphoglyceric acid (3-PGA) is described. The preparation is free of acid phosphatase and phosphoglycerate mutase. Enzyme activity is enhanced 37-fold by 20mM bisulfite. Dithionite and cyanide also cause stimulation. The pH optimum is 7.5 and the Km for 2,3-DPG is 4×10-5M. Enzyme activity is inhibited by both 3-PGA and 2-PGA. It is believed that this enzyme, and not PGA mutase which in the presence of inorganic pyrophosphate has this same phosphatase activity, is the physiological intracellular phosphatase for 2,3-DPG in erythrocytes. © 1969.

引用

页码：849 / &

共 18 条

[1]

AMES BN, 1960, J BIOL CHEM, V235, P769

[2] REGULATION OF AMP DEAMINASE BY 2,3-DIPHOSPHOGLYCERIC ACID - A POSSIBLE MECHANISM FOR CONTROL OF ADENINE NUCLEOTIDE METABOLISM IN HUMAN ERYTHROCYTES [J].