Effect of manganese on the quaternary structure of human liver arginase

Carvajal, Nelson; Venegas, Alejandro; Oestreicher, Guillermo; Plaza, María Isabel Cornejo

doi:10.1016/0005-2744(71)90200-2

Cited by 46 publications

(16 citation statements)

References 11 publications

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“…Several workers!" 19 have reported that arginase is composed of four homologous subunits. However, the present study demonstrated that the molecular weight of native erythrocyte arginase was estimated to be 105000 by gel filtration on a Sephadex G-150 and that ofa subunit of the enzyme 35000 by SDS-PAGE (Fig.…”

Section: Discussionmentioning

confidence: 99%

Purification and Properties of Human Erythrocyte Arginase

Ikemoto

Tabata²,

Murachi

et al. 1989

Ann Clin Biochem

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SUMMARY. An efficient method for purification of human erythrocyte arginase was developed. This method included two new procedures, hydrophobic chromatography and immunoaffinity chromatography, and yielded 0·7 mg of homogeneous arginase protein from 2·1 L of haemolysate. The molecular weight of native arginase was estimated to be 105000 by gel filtration on a Sephadex G-150 column, and that of its subunit 35 000 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. This indicates that the native enzyme is composed of three homologous subunits. Amino acid composition of human erythrocyte arginase was found to be very similar to that of liver arginase of several other mammals. After dialysis against distilled water, the purified arginase still retained its enzymatic activity which was decreased by EDTA and reversibly restored by Mn(II) ion. A specific polyclonal antibody for use in an immunoassay was also produced. This antibody revealed one single band on immunoelectrophoretic analysis of the acetone powder extract, suggesting absence of arginase isoenzymes in human erythrocytes.

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Section: Discussionmentioning

confidence: 99%

Purification and Properties of Human Erythrocyte Arginase

Ikemoto

Tabata²,

Murachi

et al. 1989

Ann Clin Biochem

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“…The enzymes of the first group seem to have a tetrameric structure, as demonstrated for the arginase from human liver (11) and rat liver (present results). All arginases of this group exhibit very high affinity for arginine (K 2.5-9) and, as it was shown for the enzyme from liver of ox (23) and rat (22), they are not susceptible to -SH reagents.…”

Section: Two Types Of Arginase Occurring In Animalsmentioning

confidence: 61%

“…The enzyme from human liver in the presence of EDTA underwent inactivation and dissociation into subunits of 30,000 molecular weight (11). On treatment with Mn2+ the enzyme reassociated to the active tetramer.…”

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confidence: 99%

Different Species of Arginase in Animal Tissues

Porembska¹

1973

Enzyme Protein

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The arginases found in various animals were tentatively divided into two groups: one with molecular weight of 110,000–138,000 and the second with molecular weight of 225,000–276,000. Enzymes belonging to both groups were found to occur in vertebrates and invertebrates, and were not related to the type of nitrogen metabolism. Arginases of the first group have high affinity to arginine, are not susceptible to -SH reagents and occur mainly in tissues of mammals. They have probably a tetrameric structure, which has been demonstrated for rat and human liver arginase. The enzymes of this group occur in multiple forms which may be considered as isoenzymes. Arginases of the second group, with higher molecular weight, differ in their affinity to the substrate and are susceptible to - SH reagents. Differences in the course of development of arginase in rat and frog are presented.

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“…In contrast, wild-type activity remained totally unaltered even in the presence of considerably higher EDTA concentrations. In reality, preincubation with 30 mM EDTA for 60 min at 37°C, followed by extensive dialysis, was required for total inactivation of wild-type recombinant species; under these conditions, the enzyme is converted to inactive subunits which regain activity only in the presence of Mn 2þ [20,27]. Although the results in Fig.…”

Section: Resultsmentioning

confidence: 93%