Molecular forms of human-liver arginase

Bascur, Luz; Cabello, J; Véliz, Marta; González, Alina Alerm

doi:10.1016/0926-6593(66)90151-2

Cited by 42 publications

(18 citation statements)

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“…The erythrocyte line is considered to be a secondary (perhaps fortuitous) expressor of the Al isozyme predominantly found in liver, the main site of ureagenesis; earlier kinetic and immunologic studies had indicated an identity between the arginases of these two cell types (30)(31)(32). However, direct confirmation of the inferred enzyme deficiency in liver in hyperargininemia has taken somewhat longer since it requires liver biopsy, a procedure not typically mandated for diagnostic or therapeutic purposes in these patients.…”

Section: Discussionmentioning

confidence: 99%

Differential expression of the two human arginase genes in hyperargininemia. Enzymatic, pathologic, and molecular analysis.

Grody¹,

Argyle²,

Kern³

et al. 1989

J. Clin. Invest.

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Section: Discussionmentioning

confidence: 99%

Differential expression of the two human arginase genes in hyperargininemia. Enzymatic, pathologic, and molecular analysis.

Grody¹,

Argyle²,

Kern³

et al. 1989

J. Clin. Invest.

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“…This raises the question of whether the two cationic isoenzymes from both human liver and erythrocytes described in previous reports (Cabello et al, 1965;Bascur et al, 1966) are partly the result of procedural artifacts.…”

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confidence: 89%

Purification and properties of arginase from human liver and erythrocytes

Berüter¹,

Colombo²,

Bachmann³

1978

Biochemical Journal

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Arginase was isolated from human liver and erythrocytes. The purification procedure used acetone precipitation, heat-treatment, (NH4)2SO4 precipitation, DEAE-cellulose chromatography and gel filtration on Sephadex G-200 in the presence of 2-mercaptoethanol. Both enzymes migrated to the anode at pH8.3 on polyacrylamide-gel electrophoresis. After incubation at pH8.0 and 37 degrees C the purified anionic liver arginase migrated to the cathode on polyacrylamide-gel electrophoresis. It is assumed that the multiple forms of the enzyme reported in the literature are partly artifacts of the purification procedure. The liver arginase showed a mol.wt. of 107000 determined by gel filtration and a sedimentation coefficient of 5.9S. Treatment of the liver enzyme with 0.25% sodium dodecyl sulphate at pH10 demonstrated an oligomeric structure of the enzyme with a mol.wt. of the subunit of 35000. The kinetic properties determined for the purified liver arginase showed an optimum pH of 9.3 and an optimal MnCl2 concentration of 2mM. The Km for L-arginine was 10.5 mM and for L-canavanine 50mM, and L-lysine exhibited a competitive type of inhibition with a Ki of 4.4mM. L-Homoarginine was not a substrate for liver arginase.

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“…Isoenzymes of arginase with different electrical charge have been shown in various animal species, two molecular forms of arginase have been detected in human liver and erythrocytes by CM-cellulose chromatography [5,6]. We also note that two molecEnzyme.…”

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confidence: 96%

Molecular Forms of Rat‐Liver Arginase. Isolation and Characterization

Tarrab

Rodríguez

Huitrón

et al. 1974

European Journal of Biochemistry

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Debate continues over the physical characteristics and even the existence of arginase isoenzymes. This paper gives additional support for such multiplicity and reports differences in physical characteristics among the various forms. After 2500–5000‐fold purification of rat liver arginase, three molecular forms were separated on carboxymethyl‐cellulose columns and were purified 2500–5000‐fold, 800–1000‐fold and 600–1000‐fold, respectively. The molecular forms have also been identified by chromatography in the supernatant of tissue extracts. The isolation of these molecular forms by affinity chromatography, using Sepharose‐lysine as a competitive inhibitor of arginase, shows only one main form, however. Kinetic studies were done for two of the molecular forms isolated, specifically the activation energy (Ea) the energy of denaturatization (Ed), Km, pH and the effect of divalent cations were determined. Significant differences were found for the Ea, between the two molecular forms. The isolated isoenzymes are cationic at pH 5.5 and pH 8.8. However, they show different mobilities in electrophoresis. The molecular weight determination by gel filtration yields a value of 110000 to 115000 for both forms. The use of thin‐layer immunochromatography plates, a combination of molecular weight and immunodiffusion technique, gave only one peak with the same molecular weight as that determined by gel filtration. The immunological studies showed that the isoenzymes have similar antigenic determinants.

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Molecular forms of human-liver arginase

Cited by 42 publications

References 5 publications

Differential expression of the two human arginase genes in hyperargininemia. Enzymatic, pathologic, and molecular analysis.

Differential expression of the two human arginase genes in hyperargininemia. Enzymatic, pathologic, and molecular analysis.

Purification and properties of arginase from human liver and erythrocytes

Molecular Forms of Rat‐Liver Arginase. Isolation and Characterization

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