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Evidence for a less high acceptor substrate specificity of gastric histamine methyltransferase: methylation of imidazole compounds

Barth, H., Crombach, M., Schunack, W. and Lorenz, Wilfried (1980) Evidence for a less high acceptor substrate specificity of gastric histamine methyltransferase: methylation of imidazole compounds. Biochemical pharmacology 29 (10), pp. 1399-1407.

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Abstract

The transmethylation catalysed by HMT (EC 2.1.1.8)* has been considered as absolutely specific for histamine as acceptor substrate. In this investigation Nα-MH, Nα,NαDMH, spinaceamine and synthetically prepared 4-[(2-amino-ethylmercapto)-methyl]-imidazole could be identified as further methyl-group accepting substrates (optimum substrate concentration ~ 1 mM), but the yield of extractable ...

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Item type:Article
Date:1980
Institutions:Medicine > Zentren des Universitätsklinikums Regensburg > Tumorzentrum e.V.
Identification Number:
ValueType
6104965PubMed ID
Classification:
NotationType
AlkylationMESH
AnimalsMESH
Enzyme Inhibitors/pharmacologyMESH
Histamine H1 Antagonists/pharmacologyMESH
Histamine H2 Antagonists/pharmacologyMESH
Histamine N-Methyltransferase/metabolismMESH
Imidazoles/metabolismMESH
MethylationMESH
Methyltransferases/metabolismMESH
Stomach/enzymologyMESH
Substrate SpecificityMESH
SwineMESH
Dewey Decimal Classification:600 Technology > 610 Medical sciences Medicine
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Unknown
Item ID:21899
Owner only: item control page

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