Über die Arginase.

Kossel, Albrecht; Dakin, H.D.

doi:10.1515/bchm2.1904.41.4.321

Cited by 119 publications

(22 citation statements)

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“…Endogenous flux of arginine was calculated on the basis of whole-body protein degradation (8.1 g/day) in the adult rat (394 g) [58] and arginine concentration in the rat (73 mg/g of protein) [57]. 7 Data are from Yu et al [60]. Arginine synthesis in vivo [57].…”

Section: Arginine Synthesismentioning

confidence: 99%

“…Subsequently, arginine was found in 1924 to be a major amino acid in the basic proteins of fish sperm [5], and its synthesis by mammals was deduced in the classic nutrition studies of W. C. Rose and his colleagues in 1930 [6]. Although high activities of arginase, the enzyme that hydrolyses arginine to ornithine and urea, had been identified in the liver in 1904 [7], it was the discovery of the ornithine cycle (urea cycle) by Krebs and Henseleit in 1932 [8] that led to the elucidation of prominent roles of arginine in physiology and metabolic pathways.…”

Section: Introductionmentioning

confidence: 99%

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Arginine metabolism: nitric oxide and beyond

Morris

1998

Biochemical Journal

2,450

2,036

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Arginine is one of the most versatile amino acids in animal cells, serving as a precursor for the synthesis not only of proteins but also of nitric oxide, urea, polyamines, proline, glutamate, creatine and agmatine. Of the enzymes that catalyse rate-controlling steps in arginine synthesis and catabolism, argininosuccinate synthase, the two arginase isoenzymes, the three nitric oxide synthase isoenzymes and arginine decarboxylase have been recognized in recent years as key factors in regulating newly identified aspects of arginine metabolism. In particular, changes in the activities of argininosuccinate synthase, the arginases, the inducible isoenzyme of nitric oxide synthase and also cationic amino acid transporters play major roles in determining the metabolic fates of arginine in health and disease, and recent studies have identified

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Section: Arginine Synthesismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Arginine metabolism: nitric oxide and beyond

Morris

1998

Biochemical Journal

2,450

2,036

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“…Arginase was discovered in the mammalian liver in 1904 (Kossel 1904). Arginase 1 (l-arginine-urea-hydrolyase; EC 3.5.3.1) catalyzes the final step of the urea cycle, namely the hydrolysis of l-arginine to ornithine and urea.…”

Section: Introductionmentioning

confidence: 99%

Hyperargininemia due to arginase I deficiency: the original patients and their natural history, and a review of the literature

et al. 2015

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Hyperargininemia is caused by deficiency of arginase 1, which catalyzes the hydrolysis of L-arginine to urea as the final enzyme in the urea cycle. In contrast to other urea cycle defects, arginase 1 deficiency usually does not cause catastrophic neonatal hyperammonemia but rather presents with progressive neurological symptoms including seizures and spastic paraplegia in the first years of life and hepatic pathology, such as neonatal cholestasis, acute liver failure, or liver fibrosis. Some patients have developed hepatocellular carcinoma. A usually mild or moderate hyperammonemia may occur at any age. The pathogenesis of arginase I deficiency is yet not fully understood. However, the accumulation of L-arginine and the resulting abnormalities in the metabolism of guanidine compounds and nitric oxide have been proposed to play a major pathophysiological role. This article provides an update on the first patients ever described, gives an overview of the distinct clinical characteristics, biochemical as well as genetical background and discusses treatment options.

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“…(1) Arginase (L-arginine ureahydrolase, or L-arginine amidinohydrolase, EC 3.5.3.1.) is an hydrolytic enzyme that converts arginine to ornithine and urea, (2) the former being an important precursor of polyamine biosynthesis, which is necessary for cell differentiation and proliferation. (3,4) Although arginase activity is most abundant in mammalian liver, (5) it is also found in nonhepatic tissues, such as red blood cells, (6) lactating mammary glands, (7) and the kidney.…”

Section: Introductionmentioning

confidence: 99%

Development of a Sandwich ELISA Test for Arginase Measurement Based on Monoclonal Antibodies

2001

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Human arginase was purified from liver and two monoclonal antibodies (MAbs), HA1 and HA2, were produced by fusion of spleen cells from an arginase-immunized BALB/c mouse and the NS-1 myeloma cell line. Both MAbs were of the IgG3 subclass and contained the kappa light chain. HA1 inhibited arginase activity, suggesting that it binds to the arginase catalytic site. HA1 and a horseradish peroxidase-conjugated polyclonal rabbit anti-human arginase antibody were used to develop a sandwich enzyme-linked immunoadsorbent assay (ELISA) for the quantification of human arginase, which can be used in the 1 to 300 ng/mL range. Because of its sensitivity and specificity, this MAb can be successfully applied to the ELISA quantification of arginase in serum and culture supernatants.

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Über die Arginase.

Cited by 119 publications

References 0 publications

Arginine metabolism: nitric oxide and beyond

Arginine metabolism: nitric oxide and beyond

Hyperargininemia due to arginase I deficiency: the original patients and their natural history, and a review of the literature

Development of a Sandwich ELISA Test for Arginase Measurement Based on Monoclonal Antibodies

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