A. E. Myshkin and V. S. Konyaeva
Semenov Institute of Chemical Physics, Russian Academy of Sciences, ul. Kosygina 4, Moscow, 117977 Russia
Received November 24, 1995
Abstract—It was shown that equine and bovine meth- and oxyhemoglobins show considerable differences in
their coagulation properties in the presence of phenylmercury acetate and mercury acetate in a neutral Tris
buffer. Even greater differences were revealed when the results were compared with those for human oxyhemo-
globin. Considering the substantial similarity between the macrocharacteristics of human, equine, and bovine
hemoglobins, it was concluded that protein coagulation depends strongly on relatively small differences in the
interaction with mercury reagents. These findings confirmed our earlier hypothesis of high ordering of coagu-
lation of mercurized hemoglobin.
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