Enzymically inactive members of the trans-sialidase family from Trypanosoma cruzi display β-galactose binding activity

Glycobiology

Volumn 9, Issue 6, 1999, Pages 581-587

  Cremona, María Laura ^a   Campetella, Oscar ^a   Sánchez, Daniel O ^a   Frasch, Alberto C C ^a  

^a INSTITUTO DE INVESTIGACIONES BIOTECNOLÓGICAS   (Argentina)

Author keywords

Enzymatic function; Sialidase; T. cruzi; trans sialidase

Indexed keywords

AMINO ACID; GALACTOSE; GLYCOLIPID; GLYCOPROTEIN; MONOSACCHARIDE; SIALIC ACID; SIALIDASE;

AGGLUTINATION TEST; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ERYTHROCYTE; GENE MUTATION; HOST PARASITE INTERACTION; HYDROLYSIS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FAMILY; RABBIT; TRYPANOSOMA CRUZI;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; DNA PRIMERS; DNA PROBES; GALACTOSE; HEMAGGLUTINATION TESTS; MICE; MOLECULAR SEQUENCE DATA; NEURAMINIDASE; RABBITS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; SUBSTRATE SPECIFICITY; TRYPANOSOMA CRUZI;

ANIMALIA; ORYCTOLAGUS CUNICULUS; TRYPANOSOMA; TRYPANOSOMA CRUZI;

EID: 0032971645     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/9.6.581     Document Type: Article

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