Determination of the arginase activities of homogenates of liver and mammary gland: effects of pH and substrate concentration and especially of activation by divalent metal ions

Folley, S. J.; Greenbaum, A. L.

doi:10.1042/bj0430537

Cited by 35 publications

(22 citation statements)

References 8 publications

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“…The argininosuccinate synthetase and argininosuc cinate lyase activities were measured in the super natant fraction from a liver homogenate in 0.1% cetyltrimcthyl ammonium bromide solution (5) and the arginase activity in a manganese saline solution (9 g -T 1 NaCl and 6 g -1 '1 M n S0 4-1 H20 ) according to Folley and Greenbaum (9). The homogenates were centrifuged at 4,000 g for 15 min at 4 °C.…”

Section: Enzyme Assaysmentioning

confidence: 99%

Hormonal Regulation of Three Urea Cycle Enzymes in Rat Fetal Liver

Husson¹,

Vaillant²

1979

Neonatology

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The purpose of such studies is to identify the hormones that act on the developmental formation of individual urea cycle enzymes, namely argininosuccinate synthetase, argininosuccinate lyase and arginase in the rat fetal liver. The development of argininosuccinate synthetase activity which is completely blocked by the suppression of glucocorticoids in the fetal liver is affected by neither glucagon nor thyroxine. The activity of argininosuccinate lyase which is never changed by the suppression or addition of glucocorticoids, is under the influences of glucagon and thyroxine at a late fetal period and the enzyme activity can be precociously induced in utero by injection of dibutyryl cyclic AMP to fetuses. Cortisol has been shown to precociously stimulate fetal liver arginase activity after an intraperitoneal injection, but the rise in activity at the late fetal period is not completely prevented by suppression of glucocorticoid and it seems that glucagon and thyroxine may also promote its developmental formation just before birth.

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Section: Enzyme Assaysmentioning

confidence: 99%

Hormonal Regulation of Three Urea Cycle Enzymes in Rat Fetal Liver

Husson¹,

Vaillant²

1979

Neonatology

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“…One practical difficulty is the wide pH range of the urease present, which we tentatively suggest is 5-9. If the arginaSe activity is optimal at pH 9 f 0-5 (Folley & Greenbaum (1948) suggest it is 9045)~ then it may be possible to isolate an intermediate product such as urea which may be formed if the arginase is a normal monohydrolase type The only other enzyme activity concerned with urinary nitrogenous products, other than amino-acids, is uricase, an enzyme whose activity would be enhanced by the presence of the urealurease system. Uricase is present in C. rmZe in sufficient amount to cause the disappearance of 50 % of uric acid in human urine at pH 7 after 40 hr.…”

Section: Discussionmentioning

confidence: 99%

A Preliminary Study of Ammonia Production by Corynebacterium renale and some other Pathogenic Bacteria

Lovell

Harvey

1950

Journal of General Microbiology

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SUMMARY:Urease is a constituent enzyme of Corynebactmiurn rende and appears to account for the bulk of its arnmonia production. C. renale also contains an arginase and some amino-acid deaminases, but the former has not been fully characterized. Bovine urine supports the growth of a small inocdum of C. renale for a limited time but after growth has reached a maximum it diminishes rapidly and the ammonia and pH values increase. C. renale also contains uricase but its precise significance has not yet been determined.Of the other bacteria studied, C. owis has urease activity similar to C. renak, and C. p y 0 . g~ a stronger initial arginase. C. equi contains no appreciable urease or arghwe, although it tends to form ammonia from glutamine.Corynebacterium renale is the cause of a specific cystitis and pyelonephritis in cattle; the lesions in natural infections in cattle and in experimental infections in mice and rabbits after intravenous inoculation are localized in the medulla of the kidney (Lovell, 1946; Lovell & Cotchin, 1946; Feenstra, Thorp & Gray, 1949). This selective localization may, in part, be explained by the metabolic and enzyme activities of the organism, and a study of its ammonia-producing capacity was made because of the old observation that C. r e d produces ammonia when grown in urine. A preliminary test was made to confirm this by growing a strain of C. r e d in bovine urine and in peptone water containing 1 % (w/v).urea. After 48 hr. incubation at 37" flasks of uninoculated media and those in which the organism had been grown were filtered through Seitx filters and the filtrates examined for free ammonia, urea and creatine. The results are given in Table 1, and show that in bovine urine and in a urea medium C. renale breaks down the urea with the formation of free ammonia.The creatine content of the urine remained constant, but largely diminished in the urea medium probably because of the peptone present.The ammonia-producing capacity of C. re& was therefore examined and a few comparative tests made with C. ovis, C. equi, C. pyogenes and Bacteriz.bm coli. METHODSThe methods employed were : (a) Washed suspensions of C. renak prepared from growth on agar slopes were seeded into sterile urine, peptone water containing 1 yo urea, hydrolysed peptone water and peptone water. The urine was sterilized by Seitz-filtration, and the hydrolysed peptone was prepared from a stock solution which consisted of a mixture of 100 g. of Bactopeptone and 300 ml. of cone. hydrochloric acid (A.R.) which had been boiled under a reflux condenser for 48 hr. after which most of the acid had been removed by vacuum distillation; the solution was neutralized to pH 7 by NaOH, diluted to give approximately 1 yo NaCl;

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“…Liver arginase levels were determined by the method of McLean and Gurney [7] which is a modified procedure of the Folley and Greenbaum [3] technique. Ornithine transcarbamylase was measured by the microdiffusion NHS technique of Reichard and Reichard [9] modified for the analysis of liver homogenates.…”

Section: Methodsmentioning

confidence: 99%

Influence of Alcohol Feeding and a Choline Deficiency on some Enzymes of Ammonia Detoxification in the Rat Liver

Barak¹,

Hahn²,

Tuma³

et al. 1969

Digestion

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This study demonstrated that fatty infiltration of the liver produced by a choline deficient diet is accompanied by a high degree of damage to the ammonia detoxification enzymes of the liver. Assays for arginase and ornithine transcarbamylase showed a marked loss of both enzymes in livers on a choline deficient diet. No change was observed in livers from animals on a high alcohol intake with an adequate diet. Neither the alcohol intake nor the choline deficient diet changed the levels of another enzyme involved in ammonia metabolism, glutamic dehydrogenase.

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Determination of the arginase activities of homogenates of liver and mammary gland: effects of pH and substrate concentration and especially of activation by divalent metal ions

Cited by 35 publications

References 8 publications

Hormonal Regulation of Three Urea Cycle Enzymes in Rat Fetal Liver

Hormonal Regulation of Three Urea Cycle Enzymes in Rat Fetal Liver

A Preliminary Study of Ammonia Production by Corynebacterium renale and some other Pathogenic Bacteria

Influence of Alcohol Feeding and a Choline Deficiency on some Enzymes of Ammonia Detoxification in the Rat Liver

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