Types of Arginase in Rat Tissues

Abstract

Significant amounts of arginase activity were found in homogenates of submaxillary salivary gland and epididymis, as well as of liver, kidney, mammary gland, and small intestine. The isoelectric point of arginase solubilized from kidney was at pH 7.0 in contrast to that of pH 9.4 characteristic of hepatic arginase in rat. The isozymic variants of arginase in the different tissues were identified by their electrophoretic migration on polyacrylamide gels and by titration of the enzymes against antibody prepared against purified rat liver arginase. Antibody titrations confirmed the indications obtained by electrophoresis that one type of arginase is limited to hepatic tissues (and possibly submaxillary gland) while the other type is found in all other tissues. The physiological role of arginase in hepatic tissues has been previously associated with the urea cycle; the possible function of arginase in proline synthesis in other tissues remains to be substantiated.

Activities of amino acid metabolizing enzymes in the stomach and small intestine of developing rats

“…The statistical significance of the differences between groups was estimated by Student's t-test. Results and discussion. Arginase, a typical liver enzyme also found in small proportions in the intestine (Konarska and Tomaszewki, 1975) and other tissues (Reddi et al, 1975), is probably more related to polyamine synthesis and arginine removal. As in liver and kidney (Arola et al, 1982), the actual levels of its activity in the intestine were low during the lactation period studied, rising to adult levels by the time of weaning and suggesting a common regulatory system.…”

Molecular basis of argininemia. Identification of two discrete frame-shift deletions in the liver-type arginase gene.

“…Liver-type arginase is localized in the cytosol of the liver cells of ureotelic animals and in low amounts in red blood cells (1). Arginase isozyme(s) that differs from the liver-type enzyme in catalytic, molecular, and immunological properties, is present in the kidney, small intestine, brain, and lactating mammary gland (2)(3)(4)(5). We isolated cDNA and genomic clones for rat (6,7) and human (8)(9)(10) liver arginase and determined the structures.…”

Glutamate Dehydrogenase, Alanine Aminotransferase, Thymidine Kinase, and Arginase in Fetal and Adult Human and Rat Liver

“…Arginase from rat liver (and submaxillary gland) but not from any other adult rat tissue was inactivated by serum prepared against purified rat liver arginase (8,13). Table 3 shows that 80% of the arginase from adult human liver was inactivated by the antiserum.…”

“…Blanks consisted of nonincubated complete mixtures. The activation, quantitative measurements of arginase activities, antibody titrations, and polyacrylamide gel electrophoresis of cytosolic fractions have been described (8,13). Soluble extracts from livers or whole kidneys were prepared after heat activation of the whole homogenates and were used for electrophoresis and antibody titrations.…”