The effect of variation within inhibitory domains on the activity of pea protease inhibitors from the Bowman-Birk class

Protein Expression and Purification

Volumn 36, Issue 1, 2004, Pages 106-114

  Clemente, Alfonso ^a   MacKenzie, Donald A ^b   Jeenes, David J ^b   Domoney, Claire ^a  

^a JOHN INNES CENTRE   (United Kingdom)

^b INSTITUTE OF FOOD RESEARCH   (United Kingdom)

Author keywords

Aspergillus niger; Chymotrypsin; Inhibitory domains; Pisum sativum; Protease inhibitor; Recombinant protein; Trypsin

Indexed keywords

BOWMAN BIRK INHIBITOR; CHYMOTRYPSIN; RECOMBINANT PROTEIN; TRYPSIN; TRYPSIN INHIBITOR; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; ASCOMYCETES; BIOSYNTHESIS; CHEMISTRY; DRUG ANTAGONISM; ENZYMOLOGY; GENETIC POLYMORPHISM; GENETICS; METABOLISM; MOLECULAR GENETICS; PEA; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ASCOMYCOTA; CHYMOTRYPSIN; MOLECULAR SEQUENCE DATA; PEAS; PLANT PROTEINS; POLYMORPHISM, GENETIC; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TRYPSIN; TRYPSIN INHIBITOR, BOWMAN-BIRK SOYBEAN; TRYPSIN INHIBITORS;

ASPERGILLUS; ASPERGILLUS NIGER; GLYCINE MAX; PISUM; PISUM SATIVUM;

EID: 3042549582     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.03.015     Document Type: Article

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