兔脑内寡肽酶A和内寡肽酶B（脯氨酸内肽酶）对神经降压素的降解作用。
Degradation of neurotensin by rabbit brain endo-oligopeptidase A and endo-oligopeptidase B (proline-endopeptidase).
作者信息
Camargo A C, Caldo H, Emson P C
出版信息
Biochem Biophys Res Commun. 1983 Nov 15;116(3):1151-9. doi: 10.1016/s0006-291x(83)80263-0.
The degradation of neurotensin and D-Tyr11 neurotensin by apparently homogeneous preparations of rabbit brain endo-oligopeptidase A and endo-oligopeptidase B (Proline-endopeptidase) was studied. Peptide fragments were isolated by high performance liquid chromatography and identified by amino acid analysis. Endo-oligopeptidase A cleaved neurotensin at the Arg8-Arg9 bond whereas D-Tyr11 neurotensin was not significantly hydrolysed. Endo-oligopeptidase B cleaved at the carboxyl side of Pro7, Pro10 in neurotensin and at Pro7 in D-Tyr11 neurotensin. The concentration dependent inhibition of neurotensin degradation by bradykinin and vice-versa represents additional evidence that endo-oligopeptidase A cleaves both Phe5-Ser6 bond of bradykinin and the Arg8-Arg9 bond of neurotensin.
研究了兔脑内寡肽酶A和内寡肽酶B（脯氨酸内肽酶）的明显均一制剂对神经降压素和D-酪氨酸11神经降压素的降解作用。通过高效液相色谱法分离肽片段，并通过氨基酸分析进行鉴定。内寡肽酶A在精氨酸8-精氨酸9键处切割神经降压素，而D-酪氨酸11神经降压素未被显著水解。内寡肽酶B在神经降压素的脯氨酸7、脯氨酸10的羧基侧以及D-酪氨酸11神经降压素的脯氨酸7处切割。缓激肽对神经降压素降解的浓度依赖性抑制以及反之亦然，这是内寡肽酶A切割缓激肽的苯丙氨酸5-丝氨酸6键和神经降压素的精氨酸8-精氨酸9键的额外证据。
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