Domain truncation studies reveal that the streptokinase-plasmin activator complex utilizes long range protein-protein interactions with macromolecular substrate to maximize catalytic turnover

Journal of Biological Chemistry

Volumn 278, Issue 33, 2003, Pages 30569-30577

  Sundram, Vasudha ^c   Nanda, Jagpreet S ^c   Rajagopal, Kammara ^c   Dhar, Jayeeta ^c   Chaudhary, Anita ^a   Sahni, Girish ^b  

^a INDIAN AGRICULTURAL RESEARCH INSTITUTE   (India)

^b INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ESCHERICHIA COLI; PROTEINS; PURIFICATION;

STREPTOKINASE (SK);

BIOCHEMISTRY;

COMPLEMENTARY DNA; PLASMIN; PLASMINOGEN; PLASMINOGEN ACTIVATOR; RNA POLYMERASE; STREPTOKINASE;

AFFINITY CHROMATOGRAPHY; ARTICLE; ESCHERICHIA COLI; GENE EXPRESSION; KINETICS; MOLECULAR CLONING; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION;

CATALYTIC DOMAIN; DNA, COMPLEMENTARY; ESCHERICHIA COLI; HUMANS; KRINGLES; PLASMIN; PLASMINOGEN; PLASMINOGEN ACTIVATORS; PROTEIN STRUCTURE, TERTIARY; STREPTOKINASE; SUBSTRATE SPECIFICITY;

ESCHERICHIA COLI;

EID: 0042232551     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M303799200     Document Type: Article

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