[A structural-functional assessment of serum albumin in cancerous diseases]

HSA structure was studied in healthy subjects and cancer patients using infrared spectroscopy. No significant differences were observed although the intensity of valent C-H fluctuation lines in alkyl groups of HSA was slightly increased in cancer patients. Gas-liquid chromatography established changes in the profile of polyunsaturated fatty acids binding to HSA in cancer patients. The data obtained suggest inhibition of omega-6 pathway of fatty acid metabolism and activation of omega-3 pathway. Marked binding of POL products to serum albumin was found nonspecific and was considered evidence of protective function of that protein.