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dc.contributor.advisorRoon, Robert J.
dc.contributor.advisorWiens, A. Wayne
dc.contributor.authorBan, David J.
dc.date.accessioned2012-01-31T15:44:39Z
dc.date.available2012-01-31T15:44:39Z
dc.date.issued1976
dc.identifier.urihttp://hdl.handle.net/10920/24769
dc.descriptioniv, 54 p.en_US
dc.description.abstractStudies were undertaken to further characterize the constitutive internal form of asparaginase in Saccharomyces cerevisiae in terms of its genetics and biochemistry and to show that a precursor-product relationship did not exist . between this enzyme and the inducible external form found in three S. cerevisiae strains. A recombinant strain was isolated that exhibited normal external enzyme activity, but no internal enzyme activity. A rough estimate of the molecular weight from two enzyme preparations was obtained, as were data concerning temperature dependence and sensitivity, susceptibility to inhibitors and substrate specificity.en_US
dc.description.sponsorshipDepartment of Biochemistry. Medical School. University of Minnesota. Minneapolis, Minnesota.
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen_US
dc.relation.ispartofKalamazoo College Health Sciences Senior Individualized Projects Collection
dc.relation.ispartofseriesSenior Individualized Projects. Health Sciences;
dc.rightsU.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder. All rights reserved.
dc.titleStudies on the Internal and Extyernal Asparaginases of Saccharomyces Cerevistaeen_US
dc.typeThesisen_US
KCollege.Access.ContactIf you are not a current Kalamazoo College student, faculty, or staff member, email dspace@kzoo.edu to request access to this thesis.


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