Please use this identifier to cite or link to this item: http://hdl.handle.net/10125/31971

Cathepsin H: Purification and Characterization of Inhibitors from Hog Kidney

File Size Format  
biology4016.PDF 613.22 kB Adobe PDF View/Open

Item Summary

Title:Cathepsin H: Purification and Characterization of Inhibitors from Hog Kidney
Authors:Lee, Alan
Contributors:Lenney, James (advisor)
Biology (department)
Date Issued:15 Jan 2014
Publisher:University of Hawaii at Manoa
Abstract:Cathepsin H is an important lysosomal thiol proteinase recently described and differentiated from another lysosomal proteinase, cathepsin B. Both cathepsins H and B resemble papain (a thiol proteinase frpm papaya) and show optimal activity in the neutral pH range. Both are able to hydrolyze the synthetic substrate benzoyl-DL-arginine-2-naphthyl amide (BANA).
Pages/Duration:v, 34 pages
URI/DOI:http://hdl.handle.net/10125/31971
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.
Appears in Collections: Honors Projects for Biology


Please email libraryada-l@lists.hawaii.edu if you need this content in ADA-compliant format.

Items in ScholarSpace are protected by copyright, with all rights reserved, unless otherwise indicated.