Show simple item record

dc.contributor.authorMargolis, Sam Aaronen_US
dc.date.accessioned2018-06-26T15:58:01Z
dc.date.available2018-06-26T15:58:01Z
dc.date.issued1963
dc.date.submitted1963
dc.identifier.otherb14688670
dc.identifier.urihttps://hdl.handle.net/2144/29685
dc.descriptionThesis (Ph.D.)--Boston Universityen_US
dc.description.abstractEhrlich ascites carcinoma lactic acid dehydrogenase was isolated from an eleven-day old tumor by acid precipitation, ammonium sulfate fractionation, and chromatography on DEAE cellulose. Electrophoretic analysis indicated that the final enzyme preparation and the ammonium sulfate fraction contained a single isoenzyme, that is, one of the five possible forms of lactic acid dehydrogenase two of which are tetramers of a single but different protein while the other three are tetramer mixtures of both proteins (i.e. hybrid enzymes). Ultracentrifugal analysis indicated that the final enzyme preparation was composed of two major components with sedimentation rates of 7.3 S and 1.9 S. The enzymatic activity was associated only with the 7.3 S component. The apparent loss of enzymatic activity in 0.1 M phosphate buffer pH 7.0 and the magnitude of the value of the 1.9 S component indicated that this represented the subunit of the enzyme. [TRUNCATED]en_US
dc.language.isoen_US
dc.publisherBoston Universityen_US
dc.rightsBased on investigation of the BU Libraries' staff, this work is free of known copyright restrictions.en_US
dc.subjectEhrlich-Lettre ascites carcinomaen_US
dc.subjectLactate dehydrogenaseen_US
dc.subjectTumorsen_US
dc.titleEhrlich ascites carcinoma lactic acid dehydrogenase, its purification, characterization and antiserumen_US
dc.typeThesis/Dissertationen_US
etd.degree.nameDoctor of Philosophyen_US
etd.degree.leveldoctoralen_US
etd.degree.disciplineBiochemistryen_US
etd.degree.grantorBoston Universityen_US
dc.identifier.mmsid99175748490001161


This item appears in the following Collection(s)

Show simple item record