Theerasilp S, Hitotsuya H, Nakajo S, Nakaya K, Nakamura Y, Kurihara Y
Department of Chemistry, Faculty of Education, Yokohama National University, Japan.
J Biol Chem. 1989 Apr 25;264(12):6655-9.
The taste-modifying protein, miraculin, has the unusual property of modifying sour taste into sweet taste. The complete amino acid sequence of miraculin purified from miracle fruits by a newly developed method (Theerasilp, S., and Kurihara, Y. (1988) J. Biol. Chem. 263, 11536-11539) was determined by an automatic Edman degradation method. Miraculin was a single polypeptide with 191 amino acid residues. The calculated molecular weight based on the amino acid sequence and the carbohydrate content (13.9%) was 24,600. Asn-42 and Asn-186 were linked N-glycosidically to carbohydrate chains. High homology was found between the amino acid sequences of miraculin and soybean trypsin inhibitor.
味觉修饰蛋白奇甜蛋白具有将酸味转化为甜味的独特特性。通过一种新开发的方法（Theerasilp, S., 和 Kurihara, Y. (1988) J. Biol. Chem. 263, 11536 - 11539）从奇迹果中纯化得到的奇甜蛋白的完整氨基酸序列，采用自动埃德曼降解法进行了测定。奇甜蛋白是一种含有191个氨基酸残基的单一多肽。根据氨基酸序列和碳水化合物含量（13.9%）计算出的分子量为24,600。天冬酰胺42和天冬酰胺186通过N - 糖苷键与碳水化合物链相连。在奇甜蛋白和大豆胰蛋白酶抑制剂的氨基酸序列之间发现了高度同源性。
