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A3233

Sigma-Aldrich

L-Arginase from bovine liver

Protein ≥70 % by biuret, powder

Synonym(s):

L-Arginine amidinase, L-Arginine amidino-hydrolase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.77
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biological source

bovine liver

Quality Level

form

powder

specific activity

≥100 units/mg protein

composition

Protein, ≥70% biuret

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

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General description

L-arginase is also called as L-arginine amidinohydrolase. It exists in two forms, such as arginase-1 and arginase-2. Arginase-1 is present in liver cells and arginase-2 is seen usually in extrahepatic tissues like, kidney, brain, skeletal muscle,[1] small intestine and the lactating mammary gland.[2] Arginase -2 is mapped to human chromosome 14q24.1−24.3.[2]

Biochem/physiol Actions

L-Arginase is the major degradative enzyme for arginine; converts arginine to ornithine.
L-Arginase is the major degradative enzyme for arginine; converts arginine to ornithine; deficiency is associated with spasticity and motor dysfunction.
L-arginase hydrolyze L-arginine into L-ornithine and urea, which is the last step of the urea cycle in the liver of ureotelic species.[1] Arginase plays a major role in the mammalian immune system and the enzyme participates in several aspects of inflammation.[2]

Unit Definition

One unit will cause the hydrolysis of 1.0 μmole of L-arginine per minute at pH 9.5 and 37 °C.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Arginase: an emerging key player in the mammalian immune system
Munder M
British Journal of Pharmacology, 158(3), 638-651 (2009)
L-Arginase: a Medically Important Enzyme
Kumar K and Verma N
Research Journal of Pharmacy and Technology, 6(12), 1430-1430 (2013)
Yoshinori Narita et al.
Journal of immunology (Baltimore, Md. : 1950), 190(2), 812-820 (2012-12-19)
Evaluation of immune dysfunction during the tumor-bearing state is a critical issue in combating cancer. In this study, we initially found that IL-6, one of the cachectic factors, suppressed CD4(+) T cell-mediated immunity through downregulation of MHC class II by
Eva Källberg et al.
BMC immunology, 13, 69-69 (2012-12-14)
S100A9 has been shown to be important for the function of so called Myeloid Derived Suppressor Cells (MDSC). Cells with a similar phenotype are also involved in pro-inflammatory processes, and we therefore wanted to investigate the gene expression and function
Shelley B Weisser et al.
Methods in molecular biology (Clifton, N.J.), 946, 225-239 (2012-11-28)
Macrophages play a key role in the innate immune response and help to direct the acquired immune response. Early in the innate immune response, they produce reactive oxygen species and pro-inflammatory cytokines and chemokines to drive inflammation and are referred

Questions

  1. I want to use this enzyme at a neutal pH, could you please comment on the activity and how much reduction in enzyme activity and specificity would be happening due to the change in the pH?

    1 answer
    1. L-Arginase typically exhibits optimal activity at pH 9.5 and 37 °C. While the product is likely to retain some degree of potency, the enzymatic activity of this material at neutral pH has not been determined. The enzyme is known to be rapidly inactivated at pH values below 6, according to "The Reversible Inactivation of Rat-Liver Arginase at Low pH". Please see the link below, Figure 1, which shows the Inactivation of arginase at different pH values:
      https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1972.tb01809.x

      Please see the link below to review an additional article highlighting the relationship between pH and mouse liver arginase.
      https://www.jstage.jst.go.jp/article/biochemistry1922/45/12/45_12_1011/_pdf

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