Modelling, synthesis and biological activity of a BLV proteinase, made of (only) 116 amino acids

FEBS Letters

Volumn 326, Issue 1-3, 1993, Pages 237-240

  Precigoux G ^a   Geoffre, S ^a   Leonard R ^a   Llido, S ^a   Dautant, A ^a   d'Estaintot, B Langlois ^a   Picard, P ^a   Menard A ^a   Guillemain, B ^a   Hospital, M ^a  

^a UNIVERSITÉ DE BORDEAUX   (France)

Author keywords

BLV protease; Modelling; Protease activity and inhibition; Solid phase synthesis

Indexed keywords

PROTEINASE; SYNTHETIC POLYPEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; LEUKEMIA VIRUS; MOLECULAR BIOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN SYNTHESIS;

AMINO ACID SEQUENCE; ENDOPEPTIDASES; HUMAN T-LYMPHOTROPIC VIRUS 1; LEUKEMIA VIRUS, BOVINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; SUPPORT, NON-U.S. GOV'T;

EID: 0027299170     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(93)81798-5     Document Type: Article

References (17)

1. Bovine leukemia virus: purification and characterization of the aspartic protease.