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Comparative studies on thymidylate synthetase from P. berghei and mouse reticulocytes

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dc.contributor.authorSa Nga Pattanakitsakulen_US
dc.contributor.authorAdisorn Ratanaphanen_US
dc.contributor.authorPintip Ruenwongsaen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-10-12T07:47:33Z
dc.date.available2018-10-12T07:47:33Z
dc.date.issued1985-01-01en_US
dc.description.abstract1. 1. Partially purified thymidylate synthetase from Plasmodium berghei and mouse reticulocytes was characterized. 2. 2. The mol. wt of the enzyme from P. berghei was about twice that from mouse reticulocytes. 3. 3. The optimum pH of the enzyme from P. berghei was found to be 6.5-7.5 while that from the host was 7.0-8.0. 4. 4. The enzyme from P. berghei was more susceptible to pH denaturation than the enzyme from reticulocytes. 5. 5. The enzyme from both sources differed in their Kmvalues for substrates. 6. 6. The enzyme from reticulocytes was less sensitive to inhibition by substrate analogs than that from P. berghei. © 1985.en_US
dc.identifier.citationComparative Biochemistry and Physiology -- Part B: Biochemistry and. Vol.80, No.3 (1985), 583-587en_US
dc.identifier.doi10.1016/0305-0491(85)90295-0en_US
dc.identifier.issn03050491en_US
dc.identifier.other2-s2.0-0021904294en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/123456789/30745
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0021904294&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleComparative studies on thymidylate synthetase from P. berghei and mouse reticulocytesen_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0021904294&origin=inwarden_US

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