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

dc.contributor.advisor Lenney, James
dc.contributor.author Lee, Alan
dc.date.accessioned 2014-01-15T20:02:29Z
dc.date.available 2014-01-15T20:02:29Z
dc.date.issued 2014-01-15
dc.identifier.uri http://hdl.handle.net/10125/31971
dc.description.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).
dc.format.extent v, 34 pages
dc.publisher University of Hawaii at Manoa
dc.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.
dc.title Cathepsin H: Purification and Characterization of Inhibitors from Hog Kidney
dc.type Term Project
dc.type.dcmi Text
dc.contributor.department Biology
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.