Arginase Isozymes of Rat Mammary Gland, Liver, and Other Tissues

Glass, Richard D.; Knox, W. Eugene

doi:10.1016/s0021-9258(19)43572-2

Cited by 66 publications

(8 citation statements)

References 18 publications

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“…Antiserum against liver arginase was prepared by Dr. R. Glass as described by Glass & Knox (1973), and stored at -20°C. Normal serum was obtained from New Zealand rabbits.…”

Section: Animals and Tissue Preparationsmentioning

confidence: 99%

“…Soluble activated enzyme extracts, containing 1.4-7.8 units of arginase, were incubated for 0 and 45min at 37°C with 25-50,1 of control rabbit serum or antiserum against liver arginase (Glass & Knox, 1973) in total volumes of 1 .Oml. Samples (in duplicate) of 0.05 ml were removed immediately after mixing the serum with the enzyme extract and assayed for initial arginase activity.…”

Section: Antibody Precipitationmentioning

confidence: 99%

“…Previous results from our laboratory showed that kidney, intestine and mammary gland contained an isoenzyme that migrates toward the anode (Reddi etal., 1975), absent fromliver and submaxillary gland, and that extracts of kidney, intestine and manmary gland did not interact with antiserum against liver arginase (Glass & Knox, 1973;Reddi et al, 1975).…”

mentioning

confidence: 95%

“…Antiserum against liver arginase interacted with the enzyme from submaxillary gland, but did not inactivate or adsorb arginase from kidney, intestine or pancreas. The distribution ofarginase among 16 normal adult rat tissues is presented; the improved, sensitive, assay method was applicable to tissues containing as little as 0.1 % of the hepatic activity.The occurrence of at least two forms of arginase (EC 3.5.3.1) in mammalian tissues, one in liver and another in kidney and mammary gland, is well documented (Glass & Knox, 1973;Kaysen & Strecker, 1973;Reddi et al, 1975). Their distinction had rested primarily on differences found in the stabilities of the enzymes to chemical procedures (Glass & Knox, 1973;Kaysen & Strecker, 1973;Gasiorowska et al, 1970), temperature (Glass & Knox, 1973) and alkaline pH (Glass & Knox, 1973), in their interaction with antisera (Glass & Knox, 1973;Kaysen & Strecker, 1973) and their electrophoretic mobilities on starch (Farron, 1973) or polyacrylamide gels (Reddi et al, 1975).Previous results from our laboratory showed that kidney, intestine and mammary gland contained an isoenzyme that migrates toward the anode (Reddi etal., 1975), absent fromliver and submaxillary gland, and that extracts of kidney, intestine and manmary gland did not interact with antiserum against liver arginase (Glass & Knox, 1973;Reddi et al, 1975).However, only about 30% of the isoenzyme that migrated towards the anode and less than 5 % of the non-moving variant were recovered from the gels.…”

mentioning

confidence: 99%

“…The occurrence of at least two forms of arginase (EC 3.5.3.1) in mammalian tissues, one in liver and another in kidney and mammary gland, is well documented (Glass & Knox, 1973;Kaysen & Strecker, 1973;Reddi et al, 1975). Their distinction had rested primarily on differences found in the stabilities of the enzymes to chemical procedures (Glass & Knox, 1973;Kaysen & Strecker, 1973;Gasiorowska et al, 1970), temperature (Glass & Knox, 1973) and alkaline pH (Glass & Knox, 1973), in their interaction with antisera (Glass & Knox, 1973;Kaysen & Strecker, 1973) and their electrophoretic mobilities on starch (Farron, 1973) or polyacrylamide gels (Reddi et al, 1975).…”

mentioning

confidence: 99%

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The heterogeneity of arginases in rat tissues

Herzfeld

Raper

1976

Biochemical Journal

158

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Arginase reactions in rat tissues were shown to be catalysed by three isoenzymes which can be separated by bidirectional electrophoresis on polyacrylamide gels. Anodic electrophoresis reveals a migrating band (isoenzyme I) present in all-non-hepatic tissues except submaxillary gland and a non-migrating band found in all tissues. The latter is resolved by cathodic electrophoresis into isoenzymes III (characteristic of liver and submaxillary gland) and a non-moving band (isoenzyme II), present in kidney, intestine and pancreas. Sequential electrophoresis, in the two directions, of mixture of liver and kidney extracts in the same gel columns separated all three isoenzymes. Differences in the solubilization properties, heat-sensitivity and substrate specificity of arginases from different tissues could be correlated with their electrophoretic behaviour. L-Canavanine could replace arginine as substrate in extracts of kidney but not of liver. Both kidney isoenzymes hydrolysed L-canavanine equally well, whereas isoenzyme III from submaxillary gland showed only very low activity. Antiserum against liver arginase interacted with the enzyme with submaxillary gland, but did not inactivate or adsorb arginase from kidney, intestine or pancreas. The distribution of arginase among 16 normal adult rat tissues is presented; the improved, sensitive, assay method was applicable to tissues containing as little as 0.1% of the hepatic activity.

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“…Antiserum against liver arginase was prepared by Dr. R. Glass as described by Glass & Knox (1973), and stored at -20°C. Normal serum was obtained from New Zealand rabbits.…”

Section: Animals and Tissue Preparationsmentioning

confidence: 99%

Section: Antibody Precipitationmentioning

confidence: 99%

mentioning

confidence: 95%

mentioning

confidence: 99%

mentioning

confidence: 99%

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The heterogeneity of arginases in rat tissues

Herzfeld

Raper

1976

Biochemical Journal

158

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Arginase activity and other cellular events associated with epidermal hyperplasia

Redmond

Rothberg

1978

Journal Cellular Physiology

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The unknown biochemical role of arginase in epidermal metabolism was probed by examining the association of elevated arginase activity with epidermal hyperplasia and hyperkeratinization. Epidermal hyperplasia was induced experimentally by topical application of 1-decanol to the right side of male hairless mice while the contralateral side served as control. Arginase activity, incorporation of 3H-thymidine into DNA, DNA and protein content were measured in the separated control and experimental epidermis six hours and on days 1 through 5 and 7 after 1-decanol application. After six hours, the epidermis appears damaged histologically, and DNA synthesis is inhibited. By day 1, incorporation of 3H-thymidine into DNA is elevated and a new hyperplastic epidermis has formed beneath the original epidermis. Epidermal arginase is elevated two through seven days after 1-decanol application and always is associated with continuing epidermal hyperplasia. The stimulation of DNA synthesis, which parallels the induction of epidermal hyperplasia by 1-decanol, precedes the induction of epidermal arginase activity. An attempt to relate these results with polyamine synthesis and other metabolic events is made.

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Purification and physical properties of arginase from Xenopus laevis

Peiser¹,

Balinsky²

1982

J. Exp. Zool.

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Arginase from the liver of Xenopus laevis has been purified to homogeneity by heat treatment, acetone fractionation, and isoelectric focussing. The main component had an isoelectric point (I.E.P.) of 7.3; there is a minor component of I.E.P. 7.8. The molecular weight of the enzyme, as determined by gel filtration on Sephadex G200, is 76,000 daltons, substantially less than that of rat liver arginase studied concurrently. The molecular weight of the subunits, as determined by electrophoresis in sodium dodecyl sulfate, is 18,000 daltons, again less than that of rat liver arginase. The data indicate that Xenopus liver arginase, like rat liver arginase, is a tetramer. The molecular weight of arginase from adult Xenopus laevis corresponds to that from larval Rana esculenta.

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Arginase Isozymes of Rat Mammary Gland, Liver, and Other Tissues

Cited by 66 publications

References 18 publications

The heterogeneity of arginases in rat tissues

The heterogeneity of arginases in rat tissues

Arginase activity and other cellular events associated with epidermal hyperplasia

Purification and physical properties of arginase from Xenopus laevis

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