Picture of aircraft jet engine

Strathclyde research that powers aerospace engineering...

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 Strathclyde researchers involved in aerospace engineering and from the Advanced Space Concepts Laboratory - but also other internationally significant research from within the Department of Mechanical & Aerospace Engineering. Discover why Strathclyde is powering international aerospace research...

Strathprints also exposes world leading research from the Faculties of Science, Engineering, Humanities & Social Sciences, and from the Strathclyde Business School.

Discover more...

Purification of a 5-ht uptake inhibitor from the venom of cerastes vipera

Alzahaby, M. and Harvey, A.L. and Young, L.C. and Faure, G. and Rowan, E.G. (1998) Purification of a 5-ht uptake inhibitor from the venom of cerastes vipera. Toxicon, 36 (4). pp. 601-607. ISSN 0041-0101

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

Abstract

A protein that inhibits the re-uptake of 5-hydroxytryptamine into rat brain synaptosomes was isolated from the venom of the Sahara sand viper (Cerastes vipera) by gel filtration and reverse phase chromatography. It has a molecular weight of 13 739 Da and an 50 of about 50 nM for blocking uptake of 3H-5-HT into rat brain synaptosomes. It also augmented the responses to 5-HT in a smooth muscle preparation. It has phospholipase A2 activity, but it has no lytic activity as measured by its inability to release lactate dehydrogenase from rat brain synaptosomes. Determination of the N-terminal sequence revealed a similarity with a phospholipase A2 previously isolated from Cerastes cerastes venom.