Elizabeth L Ostler

Evidence for ‘lock and key’ character in an anti-phosphonate hydrolytic antibody catalytic site augmented by non-reaction centre recognition: variation in substrate selectivity between an anti-phosphonate antibody, an anti-phosphate antibody and two hydrolytic enzymes

Sonkaria, Sanjiv, Boucher, Guillaume, FLóREZ-ÁLVAREZ, José, Said, Bilal, Hussain, Syeed, Ostler, Elizabeth L., ...

The substrate selectivities of an anti-phosphonate and an anti-phosphate kinetically homogeneous polyclonal catalytic antibody preparation and two hydrolytic enzymes were compared by using...

Evidence for ‘lock and key’ character in an anti-phosphonate hydrolytic antibody catalytic site augmented by non-reaction centre recognition: variation in substrate selectivity between an anti-phosphonate antibody, an anti-phosphate antibody and two hydrolytic enzymes

Sonkaria, Sanjiv, Boucher, Guillaume, FLóREZ-ÁLVAREZ, José, Said, Bilal, Hussain, Syeed, Ostler, Elizabeth L., ...

The substrate selectivities of an anti-phosphonate and an anti-phosphate kinetically homogeneous polyclonal catalytic antibody preparation and two hydrolytic enzymes were compared by using...

Evidence that the mechanism of antibody-catalysed hydrolysis of arylcarbamates can be determined by the structure of the immunogen used to elicit the catalytic antibody

Boucher, Guillaume, Said, Bilal, Ostler, Elizabeth L., Resmini, Marina, Brocklehurst, Keith, Gallacher, Gerard

A kinetically homogeneous anti-phosphate catalytic antibody preparation was shown to catalyse the hydrolysis of a series of O-aryl N-methyl carbamates containing various substituents in the...