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pubmed-article:1970134pubmed:abstractTextIn this study the substrate specificity of a pyroglutamate aminopeptidase from synaptosomal membranes of guinea-pig brain was investigated. The enzyme was found to be specific for tripeptides, tripeptide-amides and tetrapeptides which possess the N-terminal sequence Glp-His and as such is specific for Thyrotropin Releasing Hormone or only very closely related peptides. The enzyme was found not to hydrolyse a number of analogues of Thyrotropin Releasing Hormone which have been shown to have therapeutical value in certain neuronal disorders.lld:pubmed
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pubmed-article:1970134pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1970134pubmed:articleTitleFurther characterization of the substrate specificity of a TRH hydrolysing pyroglutamate aminopeptidase from guinea-pig brain.lld:pubmed
pubmed-article:1970134pubmed:affiliationDepartment of Biochemistry, University College, Galway, Ireland.lld:pubmed
pubmed-article:1970134pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1970134pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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