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dc.contributor.advisorSun, Frank F.
dc.contributor.authorCray, William K., Jr.
dc.descriptionv, 25 p.en_US
dc.description.abstractThe enzyme, prostaglandin-9-keto reductase, has been partially purified from monkey kidney tissue. DEAE cellulose column chromatography and hydroxylapatite column chromatography were the two procedures used to purify the enzyme. Eleven-fold purification and 47% recovery of the enzyme were achieved. A simple assay was developed using spectrophotometric measurements of the disappearance of NADPH. Substrate specificity of the enzyme was found to be very broad. Changes made in the upper chain and the lower chain of the prostaglandin, effect little change in the activity of the enzyme. Changes made within the ring of the prostaglandin result in loss of activity of the enzyme. Kidney vaso-active agents, such as bradykinin, angiotensin II, and ethacrynic acid, produced no effect on the activity of the enzyme.en_US
dc.description.sponsorshipUpjohn Company, Kalamazoo, MI
dc.publisherKalamazoo Collegeen_US
dc.relation.ispartofKalamazoo College Chemistry Senior Individualized Projects Collection
dc.relation.ispartofseriesSenior Individualized Projects. Chemistry.;
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.titleIsolation and Characterization of Monkey Kidney Prostaglandin-9-Keto Reductaseen_US

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  • Chemistry Senior Individualized Projects [889]
    This collection includes Senior Individualized Projects (SIP's) completed in the Chemistry Department. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

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