Abstract:
: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.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Yokoyama K,Ohmori H,Kumon Adoi
10.1093/oxfordjournals.jbchem.a124032subject
Has Abstractpub_date
1993-02-01 00:00:00pages
236-40issue
2eissn
0021-924Xissn
1756-2651journal_volume
113pub_type
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