Petrilli P, Pucci P, Pelissier J P, Addeo F
Int J Pept Protein Res. 1987 Apr;29(4):504-8. doi: 10.1111/j.1399-3011.1987.tb02277.x.
Degradation by pig pancreatic juice of a beta-casomorphin-containing fragment (tryptic peptide corresponding to residues 49-68 of buffalo beta-casein) was investigated. The FAB/MS (fast atom bombardment mass spectrometry) technique was used to identify the fragments produced by the concerted action of pancreatic proteases. Pancreatic juice, under our experimental conditions, is not able to release beta-casomorphins or morphiceptin from the tryptic peptide sequence. Furthermore, the present report shows that the rapid hydrolysis of a peptide bond by a single protease can prevent the cleavage of peptide bonds by a different protease. Therefore the formation of some peptides in the gastrointestinal tract can depend on the protease ratio.
研究了猪胰液对含β-酪蛋白吗啡样肽片段（对应于水牛β-酪蛋白49 - 68位残基的胰蛋白酶肽）的降解作用。采用快原子轰击质谱（FAB/MS）技术鉴定胰蛋白酶协同作用产生的片段。在我们的实验条件下，胰液无法从胰蛋白酶肽序列中释放出β-酪蛋白吗啡样肽或内啡肽。此外，本报告表明，单一蛋白酶对肽键的快速水解可阻止不同蛋白酶对肽键的切割。因此，胃肠道中某些肽的形成可能取决于蛋白酶的比例。
