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Journal of Dairy Science Vol. 57 No. 8 860-864
© 1974 by American Dairy Science Association ®
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Purification and Characterization of Lamb Gastric Proteases1

R. V. Chaudhari2 and G. H. Richardson

Department of Nutrition and Food Sciences, Utah State University, Logan 84322

ABSTRACT

Proteolytic activity resembling cathepsins A, C, and D has been demonstrated in crude lamb gastric extracts. An assay involving proteolytic activity on hemoglobin following inactivation of rennin and pepsin is reported. Following ammonium sulphate fractionation, acetone precipitation, and gel filtration, a fifty-times purification of enzyme with retention of 15% activity was obtained. Purified protease resembling cathepsin D with some cathepsin C activity had a pH optimum at 3.5 and isoelectric point of 5.6.

FOOTNOTES

1 Approved by the Director of Utah Agricultural Experiment Station. Paper No. 1789.

2 Current address: c/o Safeway Stores Inc., Milk Department, Hanford, CA 93230.






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Copyright © 1974 by the American Dairy Science Association ®.