Alternative splicing of the type-IVA cyclic AMP phosphodiesterase gene provides isoform variants with distinct N-terminal domains fused to a common, soluble catalytic unit: ‘designer’ changes in Vmax, stability and membrane association

Houslay, M.D. et al. (1995) Alternative splicing of the type-IVA cyclic AMP phosphodiesterase gene provides isoform variants with distinct N-terminal domains fused to a common, soluble catalytic unit: ‘designer’ changes in Vmax, stability and membrane association. Biochemical Society Transactions, 23, pp. 393-398.

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Publisher's URL: http://www.biochemsoctrans.org/bst/023/bst0230393.htm

Abstract

Abbreviations used: cAMP, cyclic AMP; PKA, cAMP-dependent protein kinase; PDE, phosphodiesterase; Met26-RD1, RD1 lacking the N-terminal 25 amino acids; CAT, chloramphenical acetyltransferase.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Houslay, Professor Miles and Tobias, Professor Edward and Michie, Dr Alison
Authors: Houslay, M.D., Scotland, G., Pooley, L., Spence, S., Wilkinson, I., McCallum, F., Julien, P., Rena, N.G., Michie, A.M., Erdogan, S., Zeng, L., O'Connell, J.C., Tobias, E.S., and MacPhee, I.
College/School:College of Medical Veterinary and Life Sciences > Institute of Cancer Sciences
College of Medical Veterinary and Life Sciences > Institute of Neuroscience and Psychology
College of Medical Veterinary and Life Sciences > School of Medicine, Dentistry & Nursing
Journal Name:Biochemical Society Transactions
ISSN:0300-5127
ISSN (Online):1470-8752

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