Zamolodchikova T S, Sokolova E A, Aleksandrov S L, Mirgorodskaia O A, Morozov I A, Vorotyntseva T I
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Bioorg Khim. 1998 Apr;24(4):300-5.
The substrate specificity of duodenase from bovine duodenum mucosa to synthetic and natural polypeptides was studied. Amino acid residues preferential for duodenase in the P1 and P2 positions of the substrate were determined. It was shown that the enzyme is synthesized in epithelial secretory cells of duodenal (Brunner's) glands and enters, as part of the secreta, into the lumen of the duodenum. The possible role of duodenase as an activator of proenteropeptidase is discussed.
研究了来自牛十二指肠黏膜的十二指肠酶对合成和天然多肽的底物特异性。确定了底物P1和P2位置上十二指肠酶优先作用的氨基酸残基。结果表明,该酶在十二指肠(布伦纳氏)腺的上皮分泌细胞中合成,并作为分泌物的一部分进入十二指肠腔。讨论了十二指肠酶作为肠肽酶原激活剂的可能作用。