The optimal activity of a pseudozymogen form of recombinant matriptase under the mildly acidic pH and low ionic strength conditions

Journal of Biochemistry

Volumn 147, Issue 4, 2010, Pages 485-492

  Inouye, Kuniyo ^a   Yasumoto, Makoto ^a   Tsuzuki, Satoshi ^a   Mochida, Seiya ^a   Fushiki, Tohru ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Activation cleavage; Matriptase; PH and ionic strength dependences; Type II transmembrane serine protease; Zymogen activity

Indexed keywords

BUFFER; ENZYME PRECURSOR; MATRIPTASE; RECOMBINANT ENZYME; RECOMBINANT MATRIPTASE; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ACIDITY; ANIMAL CELL; ARTICLE; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME SUBSTRATE; FEMALE; HYDROLYSIS; IN VIVO STUDY; IONIC STRENGTH; NONHUMAN;

AMINO ACID CHLOROMETHYL KETONES; AMINO ACID MOTIFS; ANIMALS; ENTEROPEPTIDASE; ENZYME ACTIVATION; ENZYME PRECURSORS; HYDROGEN-ION CONCENTRATION; KINETICS; MUSCLE HYPOTONIA; OLIGOPEPTIDES; OSMOLAR CONCENTRATION; PROTEIN STRUCTURE, TERTIARY; RATS; RECOMBINANT FUSION PROTEINS; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY;

EID: 77950600391     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp190     Document Type: Article

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