Kasarda D D, Okita T W, Bernardin J E, Baecker P A, Nimmo C C, Lew E J, Dietler M D, Greene F C
Proc Natl Acad Sci U S A. 1984 Aug;81(15):4712-6. doi: 10.1073/pnas.81.15.4712.
The complete amino acid sequence for an alpha-type gliadin protein of wheat (Triticum aestivum Linnaeus) endosperm has been derived from a cloned cDNA sequence. An additional cDNA clone that corresponds to about 75% of a similar alpha-type gliadin has been sequenced and shows some important differences. About 97% of the composite sequence of A-gliadin (an alpha-type gliadin fraction) has also been obtained by direct amino acid sequencing. This sequence shows a high degree of similarity with amino acid sequences derived from both cDNA clones and is virtually identical to one of them. On the basis of sequence information, after loss of the signal sequence, the mature alpha-type gliadins may be divided into five different domains, two of which may have evolved from an ancestral gliadin gene, whereas the remaining three contain repeating sequences that may have developed independently.
从小麦(普通小麦)胚乳的一种α-型麦醇溶蛋白的克隆cDNA序列中推导得到了其完整的氨基酸序列。另一个对应约75%相似α-型麦醇溶蛋白的cDNA克隆已被测序,显示出一些重要差异。通过直接氨基酸测序也获得了A-麦醇溶蛋白(一种α-型麦醇溶蛋白组分)约97%的复合序列。该序列与来自两个cDNA克隆的氨基酸序列高度相似,并且实际上与其中一个完全相同。根据序列信息,在信号序列缺失后,成熟的α-型麦醇溶蛋白可分为五个不同结构域,其中两个可能由一个祖先麦醇溶蛋白基因进化而来,而其余三个含有可能独立发展而来的重复序列。