Lopap, a prothrombin activator from Lonomia obliqua belonging to the lipocalin family: Recombinant production, biochemical characterization and structure-function insights

Biochemical Journal

Volumn 398, Issue 2, 2006, Pages 295-302

  Reis, Cleyson Valença ^a   Andrade, Sonia Aparecida ^b   Ramos, Oscar Henrique Pereira ^a   Ramos, Celso Raul Romero ^a   Ho, Paulo Lee ^a   Batista, Isabel De Fátima Correia ^a   Chudzinski Tavassi, Ana Marisa ^a  

^a INSTITUTO BUTANTAN   (Brazil)

^b HOSPITAL SÍRIO LIBANÊS   (Brazil)

Author keywords

Catalytic lipocalin; Lipocalin; Lonomia obliqua; Lopap; Prothrombin activator; Structure function relationship

Indexed keywords

BIOCHEMISTRY; CATALYST ACTIVITY; DNA; ESCHERICHIA COLI; GENETIC ENGINEERING; HYDROLYSIS;

CATALYTIC LIPOCALIN; LIPOCALIN; LONOMIA OBLIQUA; LOPAP; PROTHROMBIN ACTIVATOR; STRUCTURE-FUNCTION RELATIONSHIP;

ENZYMES;

AMINO ACID; LIPOCALIN; PROTHROMBIN; BLOOD CLOTTING FACTOR 10; COMPLEMENTARY DNA; INSECT PROTEIN; LACTOGLOBULIN; LONOMIA OBLIQUA PROTHROMBIN ACTIVATOR PROTEASE; RECOMBINANT PROTEIN; SERINE PROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; BIOINFORMATICS; CATALYSIS; CHEMICAL ANALYSIS; CONTROLLED STUDY; DNA LIBRARY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN STRUCTURE; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; CLASSIFICATION; GENETICS; HUMAN; HYDROLYSIS; LEPIDOPTERA; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; STRUCTURE ACTIVITY RELATION;

ESCHERICHIA COLI; LONOMIA OBLIQUA;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CIRCULAR DICHROISM; DNA, COMPLEMENTARY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FACTOR X; HUMANS; HYDROLYSIS; INSECT PROTEINS; LACTOGLOBULINS; LEPIDOPTERA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTHROMBIN; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SERINE ENDOPEPTIDASES; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 33748365022     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20060325     Document Type: Article

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