FRAGMENTATION OF PROTEINS BY STAPHYLOCOCCUS-AUREUS STRAIN-V8 PROTEASE - AMMONIUM BICARBONATE STRONGLY INHIBITS THE ENZYME BUT DOES NOT IMPROVE THE SELECTIVITY FOR GLUTAMIC-ACID

被引：66

作者：

SORENSEN, SB ^{[1
]}

SORENSEN, TL ^{[1
]}

BREDDAM, K ^{[1
]}

机构：

[1] CARLSBERG LAB,DEPT CHEM,GL CARLSBERG VEJ 10,DK-2500 COPENHAGEN,DENMARK

来源：

FEBS LETTERS | 1991年 / 294卷 / 03期

关键词：

STAPHYLOCOCCUS-AUREUS; PROTEASE; SERINE ENDOPEPTIDASE; SPECIFICITY; AMINO ACID SEQUENCE ANALYSIS;

D O I：

10.1016/0014-5793(91)80667-R

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：

Staphylococcus aureus strain V8 protease is a serine endopeptidase which cleaves peptide bonds at the carboxyl side of Glu and Asp. Specific cleavage at Glu has previously been achieved in ammonium bicarbonate whereas in sodium phosphate cleavage at both Glu and Asp was observed. However, it is shown here that bicarbonate does not restrict the specificity to Glu-X bonds, it simply inhibits the enzyme. The degradation of a mixture of oxidized insulin and glucagon proceeds similarly in the two buffers, although faster in phosphate.

引用

页码：195 / 197

页数：3

共 7 条

[1] ACTION OF STAPHYLOCOCCAL PROTEINASE ON PEPTIDES OF VARYING CHAIN-LENGTH AND COMPOSITION [J].

AUSTEN, BM ;

SMITH, EL .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1976, 72 (02) :411-417

[2]

Drapeau G R, 1977, Methods Enzymol, V47, P189

[3]

DRAPEAU GR, 1972, J BIOL CHEM, V247, P6720

[4]

Hirs CHW., 1967, METHODS ENZYMOL, V11, P59, DOI [10.1016/S0076-6879(67)11008-2, DOI 10.1016/S0076-6879(67)11008-2]

[5] KINETIC INVESTIGATION OF STAPHYLOCOCCAL PROTEASE-CATALYZED HYDROLYSIS OF SYNTHETIC SUBSTRATES [J].

HOUMARD, J .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1976, 68 (02) :621-627

[6] STAPHYLOCOCCAL PROTEASE - A PROTEOLYTIC-ENZYME SPECIFIC FOR GLUTAMOYL BONDS [J].

HOUMARD, J ;

DRAPEAU, GR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1972, 69 (12) :3506-3509

[7]

MELDAL H, 1991, ANAL BIOCHEM, V195, P141

← 1 →