Chauvet J, Chauvet M T, Acher R
FEBS Lett. 1987 Jun 15;217(2):180-3. doi: 10.1016/0014-5793(87)80659-2.
The guinea pig two-domain precursor of MSEL-neurophysin and copeptin has been passed through a trypsin-Sepharose column in order to mimic the enzyme processing by a membrane-bound endopeptidase. Only two cleavages were observed located in the inter-domain sequence (at Arg-94 and Arg-98), in contrast to several additional cleavages found when free neurophysin or copeptin is subjected to soluble trypsin. Because the physiological maturation involves a single cleavage at Arg-94, both local accessibility in the precursor and narrow specificity of the enzyme are implied in the processing.
为模拟膜结合内肽酶的酶促加工过程，将豚鼠MSEL-神经垂体素和 copeptin的双结构域前体通过胰蛋白酶-琼脂糖凝胶柱。结果发现，与游离神经垂体素或copeptin经可溶性胰蛋白酶处理时出现的多处额外切割不同，该双结构域前体仅在结构域间序列处（位于Arg-94和Arg-98）出现了两处切割。由于生理成熟过程涉及在Arg-94处的单次切割，因此该加工过程暗示了前体中的局部可及性以及该酶的狭窄特异性。
