CATALASE OF THE METHYLOTROPHIC YEAST HANSENULA-POLYMORPHA - PURIFICATION AND PROPERTIES

被引：0

作者：

SYSOEV, OV ^{[1
]}

GRUZMAN, MB ^{[1
]}

IVANOV, EV ^{[1
]}

TROTSENKO, YA ^{[1
]}

机构：

[1] ACAD SCI USSR, INST MICROORGANISMS BIOCHEM & PHYSIOL, PUSHCHINO, USSR

来源：

BIOCHEMISTRY-MOSCOW | 1991年 / 56卷 / 10期

关键词：

METHYLOTROPHIC YEASTS; CATALASE; PURIFICATION; PROPERTIES;

D O I：

暂无

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 catalase of the methylotrophic Yeast Hansenula polymorpha was purified to a homogeneous state. The purification steps included fractionation with ammonium sulfate, chromatography on DEAE- and butyl- Toyopearl, and gel filtration on Ultragel AcA 44. The protein with molecular weight 232 kD consists of four identical subunits with molecular weight 60 kD and has the typical absorption spectrum for hemoproteins. The apparent K(m) with respect to H2O2 is equal to 24 mM. The enzyme has a broad pH optimum of activity - 5.8-8.5. The 3-amino-1,2,4-triazole, KCN, and NaN3 concentrations at which complete inhibition of the enzyme is observed at pH 7.0 without preincubation are 50, 3.5, and 0.15 mM, respectively. This enzyme is close in properties to the catalase purified from Candida-boidinii.

引用

页码：1313 / 1317

页数：5