Types of Arginase in Rat Tissues
Autor: | Knox We, Herzfeld A, Reddi Pk |
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Rok vydání: | 1975 |
Předmět: |
Male
Submandibular Gland Kidney Biochemistry Fetus Mammary Glands Animal Pregnancy Intestine Small medicine Animals Lactation Epididymis chemistry.chemical_classification Arginase Salivary gland Chemistry Neoplasms Experimental Small intestine Rats Isoenzymes medicine.anatomical_structure Isoelectric point Enzyme Liver Organ Specificity Urea cycle Female |
Zdroj: | Enzyme. 20:305-314 |
ISSN: | 2504-2564 0013-9432 |
DOI: | 10.1159/000458952 |
Popis: | 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 substantiated. |
Databáze: | OpenAIRE |
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