Turski W A, Lachowicz L
Department of Biochemistry II, Academy of Medicine, Lódź, Poland.
Folia Histochem Cytobiol. 1990;28(1-2):19-26.
The main peptidase PN/cutting Tyr8-Gly9 or Gly9-Leu10 bond (of sequence Glp6-Phe7-Tyr8-Gly9-Leu10-MetNH2) seems to be, at least in part, cysteine type enzyme. Cutting of Phe7-Tyr8 bond with PC enzyme is apparently negligible. Further degradation of labelled PN products seems to be accomplished with PI, being serine enzyme at least in part. Metalloenzymes, including "enkephalinase", seem to be of minor importance in hexapeptide degradation, at least in its very low concentration. Some typical inhibitors enhance the degradation what might be explained assuming that products of action of one peptidase strongly inhibit the other peptidase's action. Namely, products of PN and PI seem to inhibit PC except the hippocampal synaptosomes where the opposite is true.
主要肽酶PN/切割（序列为Glp6-Phe7-Tyr8-Gly9-Leu10-MetNH2的）Tyr8-Gly9或Gly9-Leu10键，似乎至少部分是半胱氨酸型酶。PC酶切割Phe7-Tyr8键的情况显然可以忽略不计。标记的PN产物的进一步降解似乎是由PI完成的，PI至少部分是丝氨酸酶。金属酶，包括“脑啡肽酶”，在六肽降解中似乎不太重要，至少在其浓度非常低时是这样。一些典型的抑制剂会增强降解，这可以假设一种肽酶的作用产物强烈抑制另一种肽酶的作用来解释。也就是说，PN和PI的产物似乎会抑制PC，但海马突触体的情况则相反。
