Fujii Y, Kobashi K, Nakai N
Arch Biochem Biophys. 1984 Aug 15;233(1):310-3. doi: 10.1016/0003-9861(84)90630-1.
An acid extract of rabbit liver contained M1-type pyruvate kinase inactivating activity, and was separated to three fractions. The optimal inactivation of the enzyme with Fraction II (Mr 42,000) was observed at pH 5.5, and this inactivation was completely prevented by leupeptin and antipain, but not by pepstatin. With Fraction III (Mr 22,000), on the other hand, optimal inactivation of the enzyme was observed at pH 8-9, and was not prevented by these inhibitors. The kinetic properties, with phosphoenolpyruvate, of the enzyme were changed from hyperbolic type to sigmoidal type by the limited proteolysis with Fractions II and III. The subunit molecular weight of the enzyme (57,300) was decreased to 55,800 via 56,400 in the former case and to 56,400 in the latter case.
兔肝的酸性提取物含有M1型丙酮酸激酶失活活性，并被分离成三个组分。用组分II（分子量42,000）对该酶进行最佳失活是在pH 5.5时观察到的，这种失活被亮抑酶肽和抑肽酶完全抑制，但不被胃蛋白酶抑制剂抑制。另一方面，用组分III（分子量22,000）时，该酶的最佳失活是在pH 8 - 9时观察到的，并且不被这些抑制剂抑制。通过用组分II和III进行有限的蛋白水解，该酶与磷酸烯醇丙酮酸的动力学性质从双曲线型变为S型。在前一种情况下，该酶的亚基分子量（57,300）经56,400降至55,800，在后一种情况下降至56,400。
