A Short Method for the Purification of Arginase From Ox Liver

Bach, S. J.; Hawkins, R. A.; Swaine, D.

doi:10.1042/bj0890263

Cited by 12 publications

(8 citation statements)

References 2 publications

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“…Arginase, a urea cycle enzyme with arginine-depleting activity, has been recognized since the 1960s as having potent anticancer properties [76]. In spite of this, arginase could not be developed as a medication due to its low affinity for arginine at physiological pH values and its in vivo half-life of only several minutes [77].…”

Section: Peg-arginase (Bct-100)mentioning

confidence: 99%

Emerging PEGylated drugs

Kang

DeLuca

Lee

2009

Expert Opinion on Emerging Drugs

231

194

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PEGylation is a pharmaceutical technology that involves the covalent attachment of polyethylene glycol (PEG) to a drug to improve its pharmacokinetic, pharmacodynamic, and immunological profiles, and thus, enhance its therapeutic effect. Currently, PEGylation is used to modify proteins, peptides, oligonucleotides, antibody fragments, and small organic molecules. Research groups are striving to improve the consistencies of PEGylated drugs and to PEGylate commercialized proteins and small organic molecules. Furthermore, the PEGylations of novel medications, like oligonucleotides and antibody fragments, are being pursued to improve their bioavailabilities. This active research in the PEGylation field and the continued growth of the biopharmaceutical market predicts that PEGylated drugs have a bright future.

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Section: Peg-arginase (Bct-100)mentioning

confidence: 99%

Emerging PEGylated drugs

Kang

DeLuca

Lee

2009

Expert Opinion on Emerging Drugs

231

194

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“…This lack of information prompted us to undertake a study of the molecular properties of beef liver arginase. I n the course of purifying this enzyme using two previously reported procedures [7,8] we were unable to obtain a pure and active arginase preparation suitable for such studies. The work presented here described the development of a new effective method for the purification of beef liver arginase.…”

mentioning

confidence: 98%

Beef-Liver Arginase. Isolation and Molecular Properties

Harell

Sokolovsky

1972

Eur J Biochem

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A procedure is described for the purification of arginase from extracts of beef liver. The enzyme which catalyzes the cleavage of L-arginine to ornithine and urea has been purified 630-fold, appeared to be homogeneous in the ultracentrifuge and by disc electrophoresis. The molecular weight determined by sedimentation equilibrium and amino acid analysis is 115000 & 5000. Beef liver arginase is a slightly acidic protein (PI 5.9) and binds 4 atom of Mn2f which are essential to the enzymic activity. The enzyme requires also the presence of manganese ions for stability.Arginase the terminal enzyme of the ureaornithine cycle, catalyzes the cleavage of L-arginine to ornithine and urea [l]. Arginase is present abundantly in mammalian liver [2], but small amounts of arginase are also found in the liver of uricotelic animals, in a variety of plants and in certain bacteria. There are many publications reporting differences in the properties of mammalian arginases 131 (and references cited there). The catalytic activity of arginase from different species and from different tissues has been found to depend greatly on the presence of divalent metal ions, e.g., Mn2+, Co2+, Ni2+ [4-61. Nevertheless, the role of the metal ion in the mode of action of arginase is still unclear. This lack of information prompted us to undertake a study of the molecular properties of beef liver arginase. I n the course of purifying this enzyme using two previously reported procedures [7,8] we were unable to obtain a pure and active arginase preparation suitable for such studies. The work presented here described the development of a new effective method for the purification of beef liver arginase. The enzyme obtained by this procedure has been partially characterized. EXPERIMENTAL PROCEDURE MATERIALSL-Arginine (free base) and L-ornithine-HC1 were obtained from Ajinomoto (Japan). Urea was obtained from Fisher, DEAE-cellulose (DE-52) from Whatman, SE-Sephadex C-50 from Pharmacia, Biogel P-150 (100-200mesh) and P-4 (100 to 200mesh) from Bio-Rad, MnC1,.4H,O and diacetylmonoxime (analytical grade) from Merck, arsenic acid (syrupy) from BDH. Beef livers were Enzyme. Arginase (EC 3.5.3.1). obtained a t the slaughter house, and were chilled immediately in dry ice. The livers were either immediately worked up or frozen at -20 "C. METHODS

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“…The arginine-degrading enzyme in the urea cycle is arginase, the in vitro anticancer property of which has been well documented since the 1960s (5). Arginase enzymatically converts arginine to ornithine and urea.…”

Section: Introductionmentioning

confidence: 99%