VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Phosphoprotein phosphatase of the myocardium. Isolation of individual molecular forms and their regulation

   
Parsadanian G.K., Ter-Tatevosian L.P., Aslanian I.G., Adunts G.T.
PubMed Id: 3004034
Year: 1985  Volume: 31  Issue: 5  Pages: 45-49
Individual molecular forms of phosphoprotein phosphatase (PPase) and their inhibitors of the protein nature were isolated from rat heart muscle by means of column chromatography on DEAE Sephadex A-50. All the three fractions of PPase were capable to dephosphorylate casein but did not affect pyrophosphate. PPase I dephosphorylated trimethaphosphate or casein. The enzyme molecular forms were different from each other by the value of specific activity and sensitivity to heat treatment. Two protein inhibitors eluted by buffers of different ionic strength - 0.2 M and 1.6 M - were identified. One of them was inactivated during heat treatment (95 degrees 5 min), while the second inhibitor maintained completely its activity in these conditions.
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Parsadanian G.K., Ter-Tatevosian L.P., Aslanian I.G., Adunts G.T. (1985) Voprosy meditsinskoi khimii, 31(5), 45-49.
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