Créminon C, Rholam M, Boussetta H, Marrakchi N, Cohen P
Groupe de Neurobiochimie Cellulaire et Moléculaire, Université Pierre et Marie Curie, Paris, France.
J Chromatogr. 1988 May 25;440:439-48. doi: 10.1016/s0021-9673(00)94547-3.
The selectivity and mechanism of processing at paired basic amino acids in hormone precursors was studied on several analogues of the (1-20)-aminoterminal domain of the ocytocin/neurophysin precursor in a cleavage assay by an endoprotease partially purified from bovine pituitary secretory granules. Peptide analogues with amino acid substitutions in, and around, the basic doublet were synthesized and used as substrates. The data obtained demonstrate the strict requirement of the processing enzyme for basic amino acids in tandem within a possibly preferred conformation which may be highly conserved in the aminoterminal domain of this hormone precursor.
利用从牛垂体分泌颗粒中部分纯化的一种内切蛋白酶，通过裂解试验，对催产素/神经垂体素前体（1-20）氨基末端结构域的几种类似物进行研究，以探讨激素前体中配对碱性氨基酸的加工选择性和机制。合成了在碱性双联体及其周围有氨基酸取代的肽类似物，并用作底物。所获得的数据表明，加工酶对碱性氨基酸严格要求以可能的优先构象串联排列，这种构象在该激素前体的氨基末端结构域中可能高度保守。
