DIRECT SPECTROPHOTOMETRIC MEASUREMENT OF RIBOSEPHOSPHATE ISOMERASE CATALYZED REACTION

被引：24

作者：

KNOWLES, FC

PON, MK

PON, NG

机构：

[1] Department of Biochemistry, University of California, Riverside

来源：

ANALYTICAL BIOCHEMISTRY | 1969年 / 29卷 / 01期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1016/0003-2697(69)90005-0

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A direct and continuous spectrophotometric assay for ribosephosphate isomerase has been developed. The ultraviolet absorption spectrum of the product of the ribosephosphate isomerase catalyzed transformation of ribose 5-phosphate has a wavelength of maximum absorption at 280 mμ and a molar extinction coefficient, based on previous equilibrium constant determinations, of approximately 50. The spectrophotometric assay is valid for all states of purity of ribosephosphate isomerase. With this assay procedure, the Michaelis-Menten binding constant was determined to be 4.6 × 10-3 M. © 1969.

引用

页码：40 / &

共 12 条

[1]

ANDERSON L, 1968, COMP BIOCHEM, P379

[2]

ASHWELL G, 1957, J BIOL CHEM, V226, P65

[3]

AXELROD B, 1954, J BIOL CHEM, V209, P847

[4]

DISCHE Z, 1951, J BIOL CHEM, V192, P583

[5] EFFECTS OF LIGHT INTENSITY ON PHOTOSYNTHETIC CARBOXYLATIVE PHASE ENZYMES AND CHLOROPHYLL SYNTHESIS IN GREENING LEAVES OF HORDEUM VULGARE L [J].