Beer consumption and changes in stability of human serum proteins

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 gr oups: experimental (EG) and control (CG). Nineteen volunteers of the EG con sumed 330 mL per day of beer (about 20 g of alcohol) for 30 consecutive day s. The CG volunteers consumed mineral water instead of beer. Blood samples were collected from EG and CG patients before and after the experiment. Alb umin (Alb), globulin (Glo), and methanol-precipitable proteins (MPP) from h uman 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 spectr a were used to estimate the stability of native and denatured protein fract ions before and after BC. It was found that before BC the fractions most st able to urea denaturation were G;lo, Alb, and MPP fractions. After BC in mo st of the beer-consuming patients (EG) some changes in native and denatured protein fractions were detected: a tendency to lower stability and minor s tructural deviations; These qualitative changes were more profound-in MPP t han in Alb and Glo. Thus,Glo is more resistible to alcohol influence than A lb, which in turn is more resistible than MPP. No serum:protein changes wer e detected in patients of CG;.