[Changes in physico-chemical and enzymatic properties of myosin in experimental infarct].
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Biomedical subjects
Publications and source records attributed to I G Shtrankfel'd.
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Method of scanning calorimetry of intact and denervated F-actin shows a change in thermostability of protein after denervation.
Method of circular dichroism did not indicate any changes of the secondary structure of globular and fibrillar actin from denervated skeletal muscles. The matter that some conformational changes of the aromatic residues do in fact accompany denervation was confirmed by fluorescence studies but not by CD spectra.
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Effect of superviscous state of AO stained actin in concentrated salts (KCI) significantly decreases two weeks after denervation. These changes of anomalous behaviour of stained action are partially reversible at the long time diasrophy. This phenomenon is suggested to be connected with the structural changes of "denervated" actin, which are reflected in the changes of protein electrostatic region.
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