Purification and biochemical analysis of WprA, a 52-kDa serine protease secreted by B. subtilis as an active complex with its 23-kDa propeptide

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1386, Issue 1, 1998, Pages 211-219

  Babé, Lilia M ^a   Schmidt, Brian ^a,b  

^a Axys Pharmaceuticals Inc   (United States)

^b FIBROGEN INC   (United States)

Author keywords

Bacillus subtilis; pH profile; Propeptide; Protease; Secretion; Subtilisin; WprA

Indexed keywords

SERINE PROTEINASE; SUBTILISIN;

ARTICLE; BACILLUS SUBTILIS; BINDING SITE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME PURIFICATION; HYDROLYSIS; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; BACILLUS SUBTILIS; BACTERIAL PROTEINS; BINDING SITES; CLONING, MOLECULAR; ENZYME STABILITY; HEAT; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; PROTEASE INHIBITORS; PROTEIN PRECURSORS; PROTEIN PROCESSING, POST-TRANSLATIONAL; SEQUENCE ANALYSIS; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); POSIBACTERIA;

EID: 0032575275     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00110-1     Document Type: Article

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