Poerio E, Caporale C, Carrano L, Caruso C, Vacca F, Buonocore V
Dipartimento di Agrobiologia e Agrochimica, Università della Tuscia, Viterbo, Italy.
J Protein Chem. 1994 Feb;13(2):187-94. doi: 10.1007/BF01891977.
The sequence of a trypsin inhibitor, isolated from wheat endosperm, is reported. The primary structure was obtained by automatic sequence analysis of the S-alkylated protein and of purified peptides derived from chemical cleavage by cyanogen bromide and digestion with Staphylococcus aureus V8 protease. This protein, named wheat trypsin inhibitor (WTI), which is comprised of a total of 71 amino acid residues, has 12 cysteines, all involved in disulfide bridges. The primary site of interaction (reactive site) with bovine trypsin has been identified as the dipeptide arginyl-methionyl at positions 19 and 20. WTI has a high degree of sequence identity with a number of serine proteinase inhibitors isolated from both cereal and leguminous plants. On the basis of the findings presented, this protein has been classified as a single-headed trypsin inhibitor of Bowman-Birk type.
报道了从小麦胚乳中分离出的一种胰蛋白酶抑制剂的序列。通过对S-烷基化蛋白以及经溴化氰化学裂解和金黄色葡萄球菌V8蛋白酶消化得到的纯化肽段进行自动序列分析，获得了其一级结构。这种蛋白质名为小麦胰蛋白酶抑制剂（WTI），共有71个氨基酸残基，含有12个半胱氨酸，全部参与形成二硫键。与牛胰蛋白酶相互作用的主要位点（活性位点）已确定为第19和20位的二肽精氨酰-甲硫氨酰。WTI与从谷物和豆科植物中分离出的多种丝氨酸蛋白酶抑制剂具有高度的序列同一性。基于所呈现的研究结果，该蛋白质已被归类为鲍曼-伯克型单头胰蛋白酶抑制剂。
