The Purification and Molecular Weight of Bovine Enterokinase

dc.contributor.authorFong, Lucy
dc.contributor.departmentBiology
dc.date.accessioned2014-01-15T19:57:19Z
dc.date.available2014-01-15T19:57:19Z
dc.date.issued2014-01-15
dc.description.abstractA purification procedure has been developed for bovine enterokinase. Material extruded from bovine duodena was extracted with 1% Triton-X-100. The extract was purified on a diethyl amino ethyl cellulose column run in the presence of 0.2% Triton. The eluate was loaded on to a pancreatic trypsin inhibitor- Sepharose affinity column and eluted with 0.5M KSCN. The final step of purification is gel filtration on a Sephacryl S-300 column. Yield was about 50% with about 1920 fold purification.
dc.format.extentiv, 29 pages
dc.identifier.urihttp://hdl.handle.net/10125/31908
dc.publisherUniversity of Hawaii at Manoa
dc.rightsAll UHM Honors Projects are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission from the copyright owner.
dc.titleThe Purification and Molecular Weight of Bovine Enterokinase
dc.typeTerm Project
dc.type.dcmiText

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