Portland State University. Department of Biology
Term of Graduation
Date of Publication
Master of Science (M.S.) in Biology
1 online resource (iv, 38 pages)
Arginase has been found to occur in the tentacles, gut, and body wall of Pista pacifica Berkeley. Partially purified arginase from the intestine has a molecular weight of 200,000, a Km of about 155 mM, an arginase/canavanase ratio of 22, a pH optimum of 10.5, and a temperature optimum of 60°C. In addition, P. pacifica arginase is competitively inhibited by ornithine but is not inhibited by high arginine concentrations, nor by sulfhydryl reagents. The enzyme is not stimulated by exogenous manganese and breaks down into an active subunit under harsh treatment. The subunit has a Km of about 118 mM and is also unaffected by exogenous manganese.
Polychaete arginase shows most of the properties characteristic of arginases from other animal and plant species. However, none of the characteristics observed to date can be correlated with a particular mode of nitrotelism.
In Copyright. URI: http://rightsstatements.org/vocab/InC/1.0/ This Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
O'Malley, Karen Laurel, "Characteristics of Arginase from the Terebellid Polychaete Pista pacifica Berkeley" (1973). Dissertations and Theses. Paper 1660.