Literature summary for 2.7.3.3 extracted from

Chen, H.L.; Mao, H.Y.; Cao, M.J.; Cai, Q.F.; Su, W.J.; Zhang, Y.X.; Liu, G.M.
Purification, physicochemical and immunological characterization of arginine kinase, an allergen of crayfish (Procambarus clarkii) (2013), Food Chem. Toxicol., 62, 475-484.

Search for more literature for 2.7.3.3

Cloned(Commentary)

Cloned (Comment)	Organism
DNA and amino acid sequence determination and analysis, sequence comparisons	Procambarus clarkii

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
40000	-	-	Procambarus clarkii

Organism

Organism	UniProt	Comment	Textmining
Procambarus clarkii	H6VGI2	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	-	Procambarus clarkii

Purification (Commentary)

Purification (Comment)	Organism
native enzyme from muscle by ammonium sulfate fractionation, dialysis, and anion exchange chromatography	Procambarus clarkii

Subunits

Subunits	Comment	Organism
monomer	1 * 40000, about, SDS-PAGE and mass spectrometry	Procambarus clarkii
More	enzyme three-dimensional structure simulation and modelling, epitope prediction, overview. The enzyme has seven conformational B-cell epitopes	Procambarus clarkii

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
30	44	stable at, crayfish arginine kinase easily forms aggregates at temperatures above 44°C	Procambarus clarkii

pH Stability

pH Stability	pH Stability Maximum	Comment	Organism
4	8	crayfish arginine kinase is stable at pH 4.0-8.0	Procambarus clarkii

pI Value

Organism	Comment	pI Value Maximum	pI Value
Procambarus clarkii	isoelectric focusing	-	6.5

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Release 2023.1 (January 2023)