Bernhard W R, Somerville C R
DOE Plant Research Laboratory, Michigan State University, East Lansing 48824.
Arch Biochem Biophys. 1989 Mar;269(2):695-7. doi: 10.1016/0003-9861(89)90154-9.
A class of small polypeptides, isolated from seeds of barley and millet, which had been previously identified as putative amylase inhibitors has been found to have striking amino acid sequence identity with phospholipid transfer proteins. In addition, both classes of proteins have the same molecular weight and appear to be produced by proteolytic cleavage of an amino-terminal peptide of similar size. These properties, and the lack of any known activity for the barley protein, suggest that the putative amylase inhibitors are lipid transfer proteins.
一类从大麦和粟的种子中分离出来的小多肽，先前被鉴定为假定的淀粉酶抑制剂，现已发现它们与磷脂转移蛋白具有显著的氨基酸序列同一性。此外，这两类蛋白质具有相同的分子量，并且似乎都是由大小相似的氨基末端肽经蛋白水解切割产生的。这些特性，以及大麦蛋白缺乏任何已知活性，表明假定的淀粉酶抑制剂是脂质转移蛋白。
