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Beer consumption and changes in stability of human serum proteins
Gorinstein, Shela; Caspi, Abraham; Goshev, Ivan; Moncheva, Snejana; Zemser, Marina; Weisz, Moshe; Libman, Imanuel; Lerner, Henry Tzvi; Trakhtenberg, Simon; Martin Belloso, Olga
The aim of this study was to evaluate the influence of beer consumption (BC) on the functional and structural properties of human serum proteins (HSP). Thirty-eight volunteers (after coronary bypass) were divided into two groups: experimental (EG) and control (CG). Nineteen volunteers of the EG consumed 330 mL per day of beer (about 20 g of alcohol) for 30 consecutive days. The CG volunteers consumed mineral water instead of beer. Blood samples were collected from EG and CG patients before and after the experiment. Albumin (Alb), globulin (Glo), and methanol-precipitable proteins (MPP) from human serum were denatured with 8 M urea. Fluorescence and electrophoresis were employed in order to elucidate urea-induced conformational changes and structural behavior of proteins. The measured fluorescence emission spectra were used to estimate the stability of native and denatured protein fractions before and after BC. It was found that before BC the fractions most stable to urea denaturation were Glo, Alb, and MPP fractions. After BC in most of the beer-consuming patients (EG) some changes in native and denatured protein fractions were detected: a tendency to lower stability and minor structural deviations. These qualitative changes were more profound in MPP than in Alb and Glo. Thus, Glo is more resistible to alcohol influence than Alb, which in turn is more resistible than MPP. No serum protein changes were detected in patients of CG.
2001
Cervesa
Proteïnes en nutrició humana
Electroforesi
Fluorescència
Beer
Proteins in human nutrition
Electrophoresis
Fluorescence
info:eu-repo/semantics/embargoedAccess
(c) American Chemical Society, 2001
Article
American Chemical Society
         

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