Slaughter D, Triplett E
Cell Differ. 1976 Mar;4(6):429-40. doi: 10.1016/0045-6039(76)90029-4.
Amphibian embryo trypsin inhibitor (ATI) is shown to be a temporary inhibitor in which full trypsin activity can eventually be restored. Lineweaver-Burk plots and other binding data indicate a reversible change from competitive to non-competitive inhibition during incubation of enzyme with inhibitor in the absence of substrate. The inhibitor is active while sequestered in the yolk, and the sequestered inhibitor co-purifies with lipovitellin when the yolk is fractionated. It is further demonstrated that the inhibitor slowly leaches from the yolk in a soluble form, and it is suggested that this leakage is the result of a negative feedback controlled proteolysis within the yolk. Possible interactions between ATI and endogenous trypsin-like proteases are discussed with particular regard to the potential involvement of those materials in the control of certain developmental events; notably melanogenesis.
两栖动物胚胎胰蛋白酶抑制剂（ATI）被证明是一种临时抑制剂，其中胰蛋白酶的全部活性最终可以恢复。林-贝氏图和其他结合数据表明，在没有底物的情况下，酶与抑制剂孵育期间，抑制作用从竞争性转变为非竞争性是可逆的。该抑制剂在被隔离于卵黄时具有活性，当对卵黄进行分级分离时，被隔离的抑制剂与脂卵黄磷蛋白共纯化。进一步证明，抑制剂以可溶形式从卵黄中缓慢渗出，有人认为这种渗漏是卵黄内负反馈控制的蛋白水解作用的结果。讨论了ATI与内源性类胰蛋白酶之间可能的相互作用，特别关注了这些物质在控制某些发育事件（尤其是黑色素生成）中的潜在作用。
