SummaryTne dietary effects of phytosterol and polyunsaturated fat (PUFA-fat) on the cholesterol and fatty acids levels in serum and liver of female rats were studied, with the following results.(1) Addition of 1 cholesterol with 0.25% cholic acid to a 10% butter diet increased cholesterol levels and decreased the ratio of polyunsaturated fatty acid (PUFA) to saturated fatty acid (SFA) in the serum and liver. These changes diminished upon additions of phytosterol and PUFA-fat (cod liver oil) to the 10% butter-cholesterol diet. (2) While the cholesterol-rich diet increased the fatty acid content of the liver, addition of phytosterol to the butter-cholesterol diet depressed this increase. On the other hand , addition of PUFA-fat to the butter-cholesterol diet caused an increase of total fatty acid in the liver. (3) A negative relationship was found between the cholesterol level and the ratio of PUFA to SFA in serum (r=-0 .810) and also in liver (r=-0.548). There were significant positive correlations between the values for the serum and liver cholesterol levels (r=0 .720) and also between the respective values in the ratios of PUFA to SFA (r=0.521). These results indicate that dietary phytosterol and PUFA-fat modulate the levels of cholesterol in proportion to the increase in the ratio of PUFA to SFA in both serum and liver with the cholesterol diet , and show that the changes in the values for the serum reflected in changes in the liver.
Amajor trypsin inhibitor was purified from the extract of the whole grain of foxtail millet, Setaria italica, to an electrophoretically homogeneous protein by conventional methods. This inhibitor (FMTI-II) has a molecular weight of 7500 and contains high levels of basic amino acids, acidic amino acids, proline, and half-cystine. FMTI-II inhibited bovine and hog trypsins in a 1 : 1 (m/m) stoichiometry: the K{ values were 3.0 x 10~1l mand 2.2 x 10~10 m, respectively. Bovine a-chymotrypsin, subtilisin BPN', hog pepsin, and papain were not inhibited. The inhibitor was stable in a wide range of pH and was heatresistant at acidic pH. The chemical modification suggested that FMTI-II had a Lys-X bond as a trypsin reactive-site. FMTI-II resembles rice bran and wheat germ trypsin inhibitors, showing that it is a Bowman-Birk type inhibitor. Proteins with the ability to inhibit proteinases are widely distributed among cereal grains including barley, rye, wheat, corn, sorgham, oats, and rice, and a number of proteinase inhibitors have been purified and characterized.^These inhibitors are probably important physiologically and some inhibitors may have nutritional significance. They also serve as excellent models for the research on protein-protein interaction. Furthermore, the comparison of inhibitors from various cereals may contain information on the evolution of cereal proteins.
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