Biopolym. Cell. 1999; 15(1):18-22.
http://dx.doi.org/10.7124/bc.000500
Structure and Function of Biopolymers
The influence of pH alteration and pharmacological modulators of adenylate cyclasie system on human serum albumin conformation
1Luik A. I., 1Naboka Yu. N., 1Mogilevich S. M., 1Hushcha T. O., 2Mishchenko N. I.
  1. Institute of Bioorganic Chemistry and Petrochemistry, NAS of Ukraine
    1, Murmans'ka Str., Kyiv, Ukraine, 02094
  2. Department of Chemistry
    KU Leuven
    Celestijnenlaan 200F-B-3001, Heverlee, Belgium

Abstract

Using the dynamic light scattering method It was found that albumin glohule has the most compact configuration (Stokes diameter 59–62 Å) at physiological pH 7.4. The changes in pH, both increase to 8.0 and decrease to 5.4, resulted in the growth of globule size to 72–81 Å. At acidic shift of pH an additional peak arose in the correlation spectra caused by the light scattering on the structures with the Stokes diameters of 29–37 Å. Those conform to the sizes of the albumin subdomains. The indicated peak is not displayed at basic shift of pH. The interaction with propranolol, clonidine and carbachol, which hinder adenytate cyclase signaling system of a cell initiated structural rearrangements similar to acidic transitions. Isoproterenol, yohimbine and theophylline, which activate AdC, caused the conformaiional changes of HSA similar to basic transition.
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