PARTIAL PURIFICATION AND CHARACTERIZATION OF PEPTIDE HYDROLASES FROM GERMINATED WHEAT

被引：22

作者：

PRENTICE, N

BURGER, WC

MOELLER, M

机构：

[1] Barley and Malt Laboratory, Crops Research Division, Agricultural Research Service, U.S. Department of Agriculture, Madison, Wisconsin1 1 The work of the Barley and Malt Laboratory is supported in part by a research grant from the Malting Barley Improvemen

来源：

PHYTOCHEMISTRY | 1968年 / 7卷 / 11期

关键词：

D O I：

10.1016/S0031-9422(00)90749-0

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：

Peptide hydrolases from germinated wheat were purified by methods developed previously for barley peptide hydrolases. Comparisons of the wheat enzymes for their thermal stability, pH optima, stability at various pH values, kinetic constants, and effects of metal ions revealed that wheat possesses a neutral peptide hydrolase with properties very similar to those of barley hydrolase B. After considerable purification the acidic peptide hydrolase fraction of wheat appeared to contain two peptide hydrolases, one that was similar to barley peptide hydrolase A and a second which was more resistant to low pH and thermal denaturation. © 1968.

引用

页码：1899 / &

共 7 条

[1] PARTIAL PURIFICATION AND CHARACTERIZATION OF BARLEY PEPTIDE HYDROLASES [J].