Purification and characterization of a stable cysteine protease Ervatamin B, with two disulfide bridges, from the latex of Ervatamia coronaria

Journal of Agricultural and Food Chemistry

Volumn 48, Issue 2, 2000, Pages 171-179

  Kundu, Suman ^a   Sundd, Monica ^a   Jagannadham, Medicherla V ^a  

^a BANARAS HINDU UNIVERSITY   (India)

Author keywords

Cysteine protease; Ervatamia coronaria; Ervatamin A,B,C; Plant endopeptidase; Plant latex

Indexed keywords

CYSTEINE PROTEINASE; DISULFIDE; ERVATAMIN B; LATEX; MEDICINAL PLANT; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME ISOLATION; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; ISOELECTRIC FOCUSING; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; PH; TEMPERATURE;

AMINO ACID SEQUENCE; CYSTEINE ENDOPEPTIDASES; DISULFIDES; HYDROGEN-ION CONCENTRATION; ISOELECTRIC FOCUSING; LATEX; MOLECULAR SEQUENCE DATA; PLANTS, MEDICINAL; SUBSTRATE SPECIFICITY; TEMPERATURE;

ERVATAMIA; FELIS CATUS; TABERNAEMONTANA DIVARICATA;

EID: 0034003649     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf990661j     Document Type: Article

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