The Purification and Molecular Weight of Bovine Enterokinase
Date
2014-01-15
Authors
Contributor
Advisor
Department
Instructor
Depositor
Speaker
Researcher
Consultant
Interviewer
Narrator
Transcriber
Annotator
Journal Title
Journal ISSN
Volume Title
Publisher
University of Hawaii at Manoa
Volume
Number/Issue
Starting Page
Ending Page
Alternative Title
Abstract
A 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.
Description
Keywords
Citation
Extent
iv, 29 pages
Format
Geographic Location
Time Period
Related To
Related To (URI)
Table of Contents
Rights
All 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.
Rights Holder
Local Contexts
Collections
Email libraryada-l@lists.hawaii.edu if you need this content in ADA-compliant format.