Conformation studies with polypeptides by rotatory dispersion and thin-film dialysis.
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The method of residementation with trichloracetic acid followed by dissolution in ethanol of preparations of the human serum albumin with changed conformation under conditions of pathology was suggested for determining the amount of modified albumin. The conformationally changed albumin is separated by the mentioned method and it changes to the insoluble form. According to the content of albumin in the sediment it is possible to estimate the amount of the modified part of this protein which was determined previously by the labour-consuming method of optical rotation dispersion.
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