Welcome to the upgraded MacSphere! We're putting the finishing touches on it; if you notice anything amiss, email macsphere@mcmaster.ca

Studies on Purification and Properties of Some Halophilic Enzymes

dc.contributor.advisorBayley, S.T.en_US
dc.contributor.authorPater, Alanen_US
dc.contributor.departmentBiologyen_US
dc.date.accessioned2014-06-18T17:01:58Z
dc.date.available2014-06-18T17:01:58Z
dc.date.created2009-08-31en_US
dc.date.issued1976-04en_US
dc.description.abstract<p>The methods of affinity chromatography, heat treatment, and chromatography on agarose with (NH4)2SO4 were used in the presence of high salt concentrations to purify halophilic enzymes. The emphasis was on the purification of tryptophanase and tryptophanyl-tRNA ligase.</p> <p>Tryptophanyl-tRNA ligase was purified to homogeneity and its molecular weight and amino acid composition was determined. Its kinetic properties were examined. The properties of this halophilic enzyme were compared to the properties reported for non-halophilic tryptophanyl-tRNA ligases.</p>en_US
dc.description.degreeDoctor of Philosophy (PhD)en_US
dc.identifier.otheropendissertations/787en_US
dc.identifier.other1811en_US
dc.identifier.other983712en_US
dc.identifier.urihttp://hdl.handle.net/11375/13036
dc.subjectBiologyen_US
dc.subjectBiologyen_US
dc.titleStudies on Purification and Properties of Some Halophilic Enzymesen_US
dc.typethesisen_US

Files

Original bundle

Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
fulltext.pdf
Size:
3.95 MB
Format:
Adobe Portable Document Format