Hayakawa Y, Jahagirdar A P, Yaguchi M, Downer R G
Institute of Low Temperature Science, Hokkaido University, Sapporo, Japan.
J Biol Chem. 1989 Sep 25;264(27):16165-9.
An endogenous proteinaceous inhibitor of trehalase (alpha,alpha-trehalose-1-glucohydrolase: EC 3.2.1.28) has been isolated and purified from the serum of resting adult American cockroaches, Periplaneta americana. Purification procedures involved decreasing ionic strength, gel filtration, and reversed phase high performance liquid chromatography. Homogeneity was confirmed by polyacrylamide gel electrophoresis and end group analysis. The purified protein inhibited trehalase activity in a dose-dependent manner and was estimated to have a molecular weight of 86,000 and to contain sugar chains. An automated gas-phase sequencer was used to determine the following sequence for the N-terminal amino acid residues: H-Ala-Ilu-Pro-Thr-Pro-His-Val-Tyr-Lys-Val-X-Val-Pro-Asp-Gly-Ala-Le u-Asn-Asp.
一种内源性海藻糖酶（α,α-海藻糖-1-葡萄糖水解酶：EC 3.2.1.28）抑制剂已从成年静止美洲大蠊（Periplaneta americana）的血清中分离并纯化出来。纯化步骤包括降低离子强度、凝胶过滤和反相高效液相色谱。通过聚丙烯酰胺凝胶电泳和端基分析确认了其纯度。纯化后的蛋白质以剂量依赖方式抑制海藻糖酶活性，估计分子量为86,000，且含有糖链。使用自动气相测序仪确定了N端氨基酸残基的以下序列：H-丙氨酸-异亮氨酸-脯氨酸-苏氨酸-脯氨酸-组氨酸-缬氨酸-酪氨酸-赖氨酸-缬氨酸-X-缬氨酸-脯氨酸-天冬氨酸-甘氨酸-丙氨酸-亮氨酸-天冬酰胺-天冬氨酸。
