Isolation of N -Phosphoarginine Hydrolase from Rat Liver and Its Physical Properties1

Autor:	Hitoshi Ohmori, Akira Kumon, Kyoko Yokoyama
Rok vydání:	1993
Předmět:	chemistry.chemical_classification Chromatography Molecular mass Phosphatase Peptide General Medicine Biology Biochemistry Sedimentation coefficient Column chromatography Enzyme chemistry Sephadex Hydrolase Molecular Biology
Zdroj:	The Journal of Biochemistry. 113:236-240
ISSN:	1756-2651 0021-924X
DOI:	10.1093/oxfordjournals.jbchem.a124032
Popis:	N omega-Phosphoarginine hydrolase from rat liver cytosol was purified to apparent homogeneity on SDS-PAGE, by employing column chromatographies on Sephadex G-75, DEAE-cellulose, QAE-Toyopearl, and glutathione-2-pyridyl-disulfide-Superose. One milligram protein of the final preparation released 4 mumol/min of inorganic phosphate from N omega-phosphoarginine. The molecular mass on SDS-PAGE, the Stokes' radius and the sedimentation coefficient were estimated to be 17.3 kDa, 1.63 nm, and 2.0 s, respectively, indicating that this enzyme consists of a single peptide. The stability of the enzyme to heat depended on the buffers employed and treatment of the enzyme preparation in 50 mM Tris-HCl, pH 7.0 at 50 degrees C, reduced the hydrolytic activity with a decay constant of 0.099 per min.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::82cd2fb30d64cddd72dcbb0dd8160f63 https://doi.org/10.1093/oxfordjournals.jbchem.a124032 Zobrazit plný text záznamu