Publication:
Substrate specificity and heterogeneity of N-methyltransferases

dc.contributor.authorAmnuay Thithapandhaen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-03-12T08:41:22Z
dc.date.available2018-03-12T08:41:22Z
dc.date.issued1972-04-28en_US
dc.description.abstractHistamine N-methyltransferase ( EC. 2.1.1.8 ) from cat intestine and guinea pig brain was compared with indoleamine N-methyltransferase from rabbit lung and chick brain. Histamine N-methyltransferase, regardless of its source, methylated specifically histamine and not other imidazoles or aromatic amines. In contrast, indoleamine N-methyltransferase from rabbit lung had different substrate specificity from that of chick brain enzyme. The best substrate for lung indoleamine N-methyltransferase was N-methyltryptamine whereas serotonin was the best substrate for the chick brain enzyme. Both histamine N-methyltransferase and indoleamine N-methyltransferase appeared to occur in these species in multiple forms. They had different kinetic parameters, different pH optimum values, displayed different response towards inhibitors, and had different heat stability. © 1972.en_US
dc.identifier.citationBiochemical and Biophysical Research Communications. Vol.47, No.2 (1972), 301-308en_US
dc.identifier.doi10.1016/0006-291X(72)90712-7en_US
dc.identifier.issn10902104en_US
dc.identifier.issn0006291Xen_US
dc.identifier.other2-s2.0-0015526796en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/10000
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0015526796&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleSubstrate specificity and heterogeneity of N-methyltransferasesen_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0015526796&origin=inwarden_US

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