Characterization of the hydrolytic activity of a polyclonal catalytic antibody preparation by pH-dependence and chemical modification studies: Evidence for the involvement of Tyr and Arg side chains as hydrogen-bond donors

Biochemical Journal

Volumn 326, Issue 1, 1997, Pages 279-287

  Resmini, Marina ^a,d   Vigna, Roberta ^a,d   Simms, Caroline ^b   Barber, Nicola J ^a,b   Hagi Pavli, Eleni P ^a   Watts, Aaron B ^a   Verma, Chandra ^c   Gallacher, Gerard ^b   Brocklehurst, Keith ^a  

^a QUEEN MARY UNIVERSITY OF LONDON   (United Kingdom)

^b UNIVERSITY OF BRIGHTON   (United Kingdom)

^c UNIVERSITY OF YORK   (United Kingdom)

^d UNIVERSITY OF MILAN   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; CATALYTIC ANTIBODY; HYDROLASE; HYDROXIDE; POLYCLONAL ANTIBODY; TYROSINE;

ANTIGEN BINDING; ARTICLE; CHEMICAL MODIFICATION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME SUBSTRATE; HYDROGEN BOND; HYDROLYSIS; MICHAELIS MENTEN KINETICS; NONHUMAN; PH; PRIORITY JOURNAL; SHEEP;

ANIMALS; ANTIBODIES; ARGININE; CARBONATES; CATALYSIS; ENZYME-LINKED IMMUNOSORBENT ASSAY; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; SHEEP; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TYROSINE;

FELIS CATUS; OVIS ARIES;

EID: 0030983982     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3260279     Document Type: Article

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