Picture of virus under microscope

Research under the microscope...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

Explore SIPBS research

On the specificity of reactions catalysed by the antibody H11

Khalaf, Abedawn I. and Linaza, Sabin and Pitt, Andrew R. and Stimson, William H. and Suckling, Colin J. (2000) On the specificity of reactions catalysed by the antibody H11. Tetrahedron, 56 (3). pp. 489-495. ISSN 0040-4020

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

The substrate specificity and the stereochem. course of the reactions catalyzed by the antibody H11 (which was raised to a protein conjugated deriv. of the adduct of 1-acetoxy-buta-1,3-diene 1) have been investigated. The antibody shows high selectivity for acetoxybutadiene which it hydrolyzes to the corresponding dienol, the major diene component of the cycloaddn. reactions obsd. However, it tolerates a range of N-alkylmaleimides. The stereochem. course of cycloaddn. is shown to produce a significant enantiomeric excess of the 3aR,4S,7aR-endo-diastereoisomer by anal. with Mosher's ester derivs. This study also revealed that H11 is capable of slowly catalyzing the hydrolysis of N-alkylmaleimide substrates. The implications for the mechanism of action of H11 are discussed. [on SciFinder(R)]