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Partial Purification and Characterization of a New Hog Kidney Dipeptidase
|Title:||Partial Purification and Characterization of a New Hog Kidney Dipeptidase|
|Date Issued:||15 Jan 2014|
|Publisher:||University of Hawaii at Manoa|
|Abstract:||Homocarnosine (γ-aminobutyryl-L-histidine), a naturally occurring dipeptide in mammals, is usually assumed to be hydrolyzed by the enzyme carnosinase. Recently, it was shown that purified hog kidney carnosinase actually did not hydrolyze homocarnosine. To date, no hydrolytic enzyme for homocarnosine has been published. The hog kidney dipeptidase described in this paper is a metalloenzyme, which was partially purified by 600-fold, characterized and shown to hydrolyze homocarnosine. The activating metal was Co2+ and FDTA inhibition is fully reversible by excess Co2+ and by no other metal ion. The Km value for homocarnosine was 0.058 mM and pH 7. 2 gave optimum activity. The molecular weight of the enzyme was estimated to be 69,000. Of the substrates tested, anserine, carnosine, β-alanylalanine, glycyl-histidine and homocarnosine were hydrolyzed, but not glycyl-leucine, indicating it is not an ordinary dipeptidase. Compared with carnosinase, the properties of this enzyme are very different.|
|Pages/Duration:||iv, 37 pages|
|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|
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