Hoffmann T, Faust J, Neubert K, Ansorge S
Department of Internal Medicine, Otto-von-Guericke-University Magdeburg, Germany.
FEBS Lett. 1993 Dec 20;336(1):61-4. doi: 10.1016/0014-5793(93)81609-4.
A number of natural cytokines are characterized as having dipeptidyl peptidase (DP) IV susceptible N-terminal peptide sequences. Here we demonstrate that oligopeptides with sequences analogous to the N-terminal part of human IL-1 beta, IL-2, TNF-beta and murine IL-6 were hydrolyzed by purified DP IV and aminopeptidase N (AP-N). The rate of DP IV-catalyzed hydrolysis of these peptides was negatively correlated with their chain length. In contrast to these results, no degradation was found under our conditions for the intact recombinant cytokines, IL-1 alpha, IL-1 beta, IL-2, G-CSF and for natural IL-2, independent of whether DP IV and AP-N were used separately or in combination.
许多天然细胞因子的特征是具有对二肽基肽酶（DP）IV敏感的N端肽序列。在此我们证明，具有与人IL-1β、IL-2、TNF-β和小鼠IL-6的N端部分类似序列的寡肽可被纯化的DP IV和氨肽酶N（AP-N）水解。这些肽的DP IV催化水解速率与其链长呈负相关。与这些结果相反，在我们的条件下，完整的重组细胞因子IL-1α、IL-1β、IL-2、G-CSF以及天然IL-2均未发现降解，无论单独使用还是联合使用DP IV和AP-N。
