Abstract:
:A simple method is described for the isolation of crystalline pyruvate kinase from human skeletal muscle. The enzyme was purified by ammonium sulfate fractionation, heat treatment and crystallization. Two crystal forms of pyruvate kinase differing in solubility but not in specific activity were found. The homogenous enzyme preparations in triethanolamine buffer, pH 7.6 reveal at 25 degrees a specific activity of 245 U per mg protein, and of 340 U/mg in potassium phosphate buffer (50 mM). The enzyme is activated by inorganic phosphate and fructosediphosphate to the same extent, and inhibited non competetively by ammonium ion. The molecular weight as measured by gel filtration is 220,000 daltons and the enzyme molecule is composed of 4 subunits.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Baranowska B,Baranowski Tdoi
10.1007/BF01732078subject
Has Abstractpub_date
1975-03-27 00:00:00pages
197-201issue
3eissn
0300-8177issn
1573-4919journal_volume
6pub_type
杂志文章abstract::Nuclear factor-kappaB (NF-κB) is a transcription factor that is activated in various neoplasms, including gastric cancer. Insulin-like growth factor binding protein-3 (IGFBP-3) is a potent tumor suppressor and is significantly suppressed in a variety of cancers. Although IGFBP-3 has been reported to have antiprolifera...
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journal_title:Molecular and cellular biochemistry
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更新日期:2011-08-01 00:00:00
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journal_title:Molecular and cellular biochemistry
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更新日期:2007-01-01 00:00:00
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更新日期:2015-07-01 00:00:00