Jett M F, Hers H G
Eur J Biochem. 1981 Aug;118(2):283-8. doi: 10.1111/j.1432-1033.1981.tb06398.x.
A high-speed supernatant from rat liver contains at least two latent phosphorylase phosphatases the activities of which are revealed by treatment with ethanol, urea, mercaptoethanol or trypsin. This fraction also contains at least one protein which, after heating, inhibits to various degrees the activated form(s) of the two phosphatases. The two latent enzymes can be separated by cellulase-phosphate chromatography and can be differentiated by their preferential activation by ethanol or trypsin and by their different sensitivity to the inhibitory protein after ethanol activation. Activation of the latent phosphorylase phosphatases by ethanol, urea or mercaptoethanol is not accompanied by the destruction of the precursor of the inhibitory protein whereas activation by trypsin is. However, trypsin treatment of fractions previously activated by ethanol decreases their activity and also increases their sensitivity to the inhibitory protein in a way which is unrelated to the destruction of this inhibitor. Furthermore, some protein fractions, almost free of the precursor of the inhibitory protein can be readily activated by trypsin. In is concluded that the activation of the latent phosphorylase phosphorylase phosphatases is unrelated to the destruction of the inhibitory protein.
大鼠肝脏的高速上清液中至少含有两种潜在的磷酸化酶磷酸酶，用乙醇、尿素、巯基乙醇或胰蛋白酶处理可使其活性显现。该组分还含有至少一种蛋白质，加热后，它会不同程度地抑制这两种磷酸酶的活化形式。这两种潜在的酶可以通过纤维素磷酸柱色谱法分离，并且可以通过它们对乙醇或胰蛋白酶的优先活化以及乙醇活化后对抑制性蛋白质的不同敏感性来区分。乙醇、尿素或巯基乙醇对潜在磷酸化酶磷酸酶的活化并不伴随着抑制性蛋白质前体的破坏，而胰蛋白酶的活化则会导致这种破坏。然而，用胰蛋白酶处理先前经乙醇活化的组分，会降低其活性，并以与该抑制剂破坏无关的方式增加它们对抑制性蛋白质的敏感性。此外，一些几乎不含抑制性蛋白质前体的蛋白质组分很容易被胰蛋白酶活化。由此得出结论，潜在磷酸化酶磷酸酶的活化与抑制性蛋白质的破坏无关。
