Molecular Characteristics of Rat Liver Arginase

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Molecular characteristics of rat liver arginase.

The molecular weight of approximately 1,500-fold purified arginase from rat liver (specific activity = 19,500 pmoles of urea per min at 25’ per mg of protein nitrogen) was determined by the method of sedimentation equilibrium to be 118,000. The sedimentation velocity constant is 6.1 S, the diffusion coefficient 5.2 X 10U7 cm2 per sec. Alteration in pH, removal of Mn2+, and replacement of Mn2+ b...

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On molecular sizes of rat liver arginase.

Arginase exists as 2 or more molecular species in the size profile of the soluble macromolecules of rat liver in the absence of added Mn@. The principal species is that of approximately 120,000 molecular weight, as previously re ported by others. In addition, after activation by Mn@ , there are detectable small but significant amounts of arginase of about 30,000—40,000 molecular weight, presu...

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Molecular Characteristics of Chicken Liver Arginase By ENRICO GRAZI and ERMES MAGRI

A purification procedure for the preparation of chicken liver arginase in a homogeneous form is presented. The enzyme hydrolyses both arginine and argininic acid. Kinetic analysis reveals that the enzyme binds arginine when the amino group is protonated or unprotonated; however, the unprotonated form seems to be hydrolysed more rapidly. The enzyme exchanges with the medium approx. 1.6Mn2+ ions ...

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In vitro analysis of the rat liver-type arginase promoter.

Genes for urea cycle enzymes including liver-type arginase are expressed mainly in the liver and are regulated developmentally, nutritionally, and hormonally in a coordinated manner. The promoter region of the rat arginase gene was investigated with an in vitro transcription system using nuclear extracts prepared from rat tissues. Accurate initiation of the transcription in liver nuclear extrac...

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Arginase, adenosinepyrophosphatase, and rhodanese in regenerating rat liver.

Gurd, Vars, and Ravdin (2) have shown that the restoration rate of liver protein following surgical removal of 70 per cent of the organ was greater in protein-depleted than in well nourished rats. These authors suggested that the stimulus to recovery of liver protein was more potent in the animal with the more severe reduction of liver substance. The nature of the stimulus to regeneration is no...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1968

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)94469-8