Wieser H, Seilmeier W, Belitz H D
Z Lebensm Unters Forsch. 1987 May;184(5):366-73. doi: 10.1007/BF01126659.
The peptide fractions isolated from chymotryptic hydrolysates of wheat, rye and barley prolamines [this journal (1984) 178:173] were separated into pure peptides by high-performance liquid chromatography on octadecyl silica gel. The peptides which were most abundant were analyzed for amino acid composition and in part for amino acid sequence. Besides peptides which are typical for only one of the cereals investigated, peptides of similar composition were found in all three prolamines. These contain repeating sequences and are built up of mainly Gln (Q), Pro (P) and hydrophobic amino acids (X) such as Phe, Tyr, Ile, Val and Leu. One of the most frequent partial sequences is QQPQQPXP.
从小麦、黑麦和大麦醇溶蛋白的胰凝乳蛋白酶水解产物中分离得到的肽段组分[本刊(1984年)178:173]，通过在十八烷基硅胶上进行高效液相色谱法分离成纯肽。对含量最丰富的肽段进行了氨基酸组成分析，并部分分析了氨基酸序列。除了仅在所研究的一种谷物中典型存在的肽段外，在所有三种醇溶蛋白中都发现了组成相似的肽段。这些肽段含有重复序列，主要由Gln(Q)、Pro(P)和疏水性氨基酸(X)如Phe、Tyr、Ile、Val和Leu组成。最常见的部分序列之一是QQPQQPXP。
