Abstract
Deficiency of arginase (E.C. 3.5.3.1), the fifth enzyme of the urea cycle, was found in the red blood cells (RBCs) of Macaca fascicularis monkeys (<0.2 µmol arginine cleaved/g Hb/min; normal =49.2). Liver biopsies were obtained from two of these monkeys and from one monkey with normal levels of RBC arginase activity. Arginase from both groups of animals required Mn2+ for maximal enzyme activity and demonstrated a pH optimum of 10.2 in vitro. The activity of arginase in the livers of all three monkeys was 1.1 mmol arginine cleaved/g protein/min. The apparent K m for arginine of arginase in the livers of the RBC-deficient monkeys was 7.4 and 5.9mm and in the normal monkey was 6.9mm. Similar patterns of heat denaturation were seen at 69 C without Mn2+ present and 79 C in the presence of 20mm Mn2+. No difference in mobility on either acidic or basic polyacrylamide gels for liver arginase from either RBC-deficient or normal monkeys was found. In addition, liver arginase from all three monkeys reacted similarly with anti-human liver arginase antibody. Liver arginases in RBC-deficient and normal monkeys were identical by ten criteria. These studies do not distinguish among several hypotheses for the genetic determination of arginase in different organs of this species and of man.
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This study was supported in part by the UCLA Mental Retardation Research Center and by USPHS Grants HD-11298, HD-06576, HD-04612, HD-05615, and RR-00865 and the National Foundation, March of Dimes, Grant 6-125. Mr. Terasaki was supported by a fellowship from the ARCS Foundation.
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Terasaki, K., Spector, E.B., Hendrickson, R. et al. Properties of arginase from liver of Macaca fascicularis: Comparison of normals with red blood cell arginase deficient monkeys. Biochem Genet 18, 829–841 (1980). https://doi.org/10.1007/BF00500116
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DOI: https://doi.org/10.1007/BF00500116