Hass G M, Hermodson M A, Ryan C A, Gentry L
Biochemistry. 1982 Feb 16;21(4):752-6. doi: 10.1021/bi00533a027.
The amino acid sequences of two low molecular weight proteinase inhibitors from Russet Burbank potatoes have been determined. One of these, a chymotrypsin inhibitor, is a peptide of 52 amino acid residues, while the second inhibitor, which is specific for trypsin, contains 51 amino acid residues. These peptides are highly homologous, differing at only nine positions. At position 38, the chymotrypsin inhibitor possesses leucine and the trypsin inhibitor an arginine. This difference probably represents the P1 sites, which are consistent with the respective specificities of the two inhibitors. The inhibitors are also homologous with potato inhibitor II and with an inhibitor previously isolated from eggplants.
已确定来自褐皮伯班克马铃薯的两种低分子量蛋白酶抑制剂的氨基酸序列。其中一种是胰凝乳蛋白酶抑制剂，是一个由52个氨基酸残基组成的肽，而第二种对胰蛋白酶具有特异性的抑制剂含有51个氨基酸残基。这些肽高度同源，仅在9个位置有所不同。在第38位，胰凝乳蛋白酶抑制剂含有亮氨酸，而胰蛋白酶抑制剂含有精氨酸。这种差异可能代表P1位点，这与两种抑制剂各自的特异性一致。这些抑制剂还与马铃薯抑制剂II以及先前从茄子中分离出的一种抑制剂同源。
