CHARACTERIZATION OF THE ACTIVITY AND STABILITY OF SINGLE-CHAIN CATHEPSIN-L AND PROTEOLYTICALLY ACTIVE CATHEPSIN-L CYSTATIN COMPLEXES

被引：17

作者：

DENNISON, C

PIKE, R

COETZER, T

KIRK, K

机构：

[1] Department of Biochemistry, University of Natal, Pietermaritzburg, P. O. Box 375

来源：

BIOLOGICAL CHEMISTRY HOPPE-SEYLER | 1992年 / 373卷 / 07期

关键词：

D O I：

10.1515/bchm3.1992.373.2.419

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 activity of single-chain cathepsin L was found to be markedly dependent on cysteine concentration, while a covalent, proteolytically active cathepsin L/cystatin complex was less cysteine-dependent. Cysteine levels and ionic strength did not affect the stability of either enzyme form and both enzyme forms were found to be stable for significant periods of time at or near physiological pH.

引用

页码：419 / 425

页数：7

共 11 条

[1]

BARRETT AJ, 1981, METHOD ENZYMOL, V80, P535

[2]

DENHARDT DT, 1987, ONCOGENE, V2, P55

[3] PURIFICATION AND AMINO-ACID-SEQUENCE OF CHICKEN LIVER CATHEPSIN-L [J].