Picture of person typing on laptop with programming code visible on the laptop screen

World class computing and information science research at Strathclyde...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by University of Strathclyde researchers, including by researchers from the Department of Computer & Information Sciences involved in mathematically structured programming, similarity and metric search, computer security, software systems, combinatronics and digital health.

The Department also includes the iSchool Research Group, which performs leading research into socio-technical phenomena and topics such as information retrieval and information seeking behaviour.

Explore

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)]