Hayashida S, Teramoto Y, Kira I
Department of Agricultural Chemistry, Kyushu University, Fukuoka, Japan.
Agric Biol Chem. 1991 Jan;55(1):1-6.
The enzymatically inactive but raw-starch-adsorbable peptide fragments designated as Gp-pan P and Gp-pan I were obtained from a tryptic digest of heat-inactivated hog pancreatic alpha-amylase. These two glycopeptide fragments were purified with Sephadex G-75, DEAE-Sephadex A-50, and HPLC and were found to be homogeneous on disc gel electrophoresis. Gp-pan P and I had molecular weights of 20,000 and 30,000 with SDS-PAGE, carbohydrate contents of 10% and 7%, N-terminal amino acids Gly-Trp and Ala-Val, and C-terminal amino acids Gly-Arg and Ile-Lys. Gp-pan P had promotive but Gp-pan I inhibitory effects on raw starch digestion by Aspergillus awamori var. kawachi glucoamylase I and Bacillus subtilis 65 alpha-amylase.
将热灭活的猪胰α-淀粉酶经胰蛋白酶消化后，获得了无酶活性但可吸附生淀粉的肽片段，分别命名为Gp-pan P和Gp-pan I。这两个糖肽片段经Sephadex G-75、DEAE-Sephadex A-50和高效液相色谱法纯化，在圆盘凝胶电泳中显示为均一性。SDS-PAGE分析表明，Gp-pan P和I的分子量分别为20,000和30,000，碳水化合物含量分别为10%和7%，N端氨基酸分别为Gly-Trp和Ala-Val，C端氨基酸分别为Gly-Arg和Ile-Lys。Gp-pan P对泡盛曲霉变种河合糖化酶I和枯草芽孢杆菌65α-淀粉酶的生淀粉消化有促进作用，而Gp-pan I则有抑制作用。
