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Biochemical and Biophysical Research Communications

Volumn 269, Issue 3, 2000, Pages 732-736

Equistatin, a protease inhibitor from the sea anemone Actinia equina, is composed of three structural and functional domains

(8) Štrukelj, Borut a,b Lenarčič, Brigita b Gruden, Kristina b Pungerčar, Jože b Rogelj, Boris b Turk, Vito b Bosch, Dirk c Jongsma, Maarten A c

a JO EF STEFAN INSTITUTE (Slovenia)

b UNIVERSITY OF LJUBLJANA (Slovenia)

c WAGENINGEN UNIVERSITY (Netherlands)

Author keywords

Cathepsin D; cDNA; Cysteine proteinase; Equistatin; Escherichia coli; Expression; Inhibitor; Papain; Periplasmic space

Indexed keywords

COMPLEMENTARY DNA; EQUISTATIN; PAPAIN; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN; SIGNAL PEPTIDE; THYROGLOBULIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CODON; CONTROLLED STUDY; ENZYME INHIBITION; ESCHERICHIA COLI; GENE ISOLATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN STRUCTURE; SEA ANEMONE;

ACTINIA EQUINA; ACTINIARIA; ANEMONE; ESCHERICHIA COLI; EUKARYOTA;

EID: 17444447261 PISSN: 0006291X EISSN: None Source Type: Journal
DOI: 10.1006/bbrc.2000.2356 Document Type: Article

Times cited : (38)

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