Legumain forms from plants and animals differ in their specificity

Biological Chemistry

Volumn 382, Issue 6, 2001, Pages 953-959

  Rotari, V I ^a   Dando, P M ^a   Barrett, A J ^a  

^a BABRAHAM INSTITUTE   (United Kingdom)

Author keywords

Asparaginyl endopeptidase; Specificity

Indexed keywords

ALANINE DERIVATIVE; AMIDE; AMINO ACID; AROMATIC AMIDE; ASPARAGINE DERIVATIVE; ASPARTIC ACID DERIVATIVE; BENZYLOXYCARBONYLALANYLASPARAGINYL AMINOMETHYLCOUMARYLAMIDE; CARBONYL DERIVATIVE; COUMARIN DERIVATIVE; CYSTATIN; CYSTEINE PROTEINASE; EGG WHITE; LEGUMAIN; NEUROTENSIN; PHASEOLINONE; TETANUS TOXOID; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; BEAN; CHEMICAL BOND; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STABILITY; HYDROLYSIS; HYDROPHOBICITY; MAMMAL; NONHUMAN; PH MEASUREMENT; PLANT SEED; PRIORITY JOURNAL; SWINE;

AMINO ACID SEQUENCE; ANIMALS; ASPARAGINE; CYSTEINE ENDOPEPTIDASES; HEMOGLOBINS; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KIDNEY; MOLECULAR SEQUENCE DATA; PHASEOLUS; PLANT PROTEINS; SEEDS; SUBSTRATE SPECIFICITY; SWINE; TETANUS TOXOID;

ANIMALIA; MAMMALIA; PHASEOLUS (ANGIOSPERM); PHASEOLUS VULGARIS; SUS; SUS SCROFA;

EID: 0034925333     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2001.119     Document Type: Article

References (33)

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