Beaudoin A R, Vachereau A, St-Jean P
Biochim Biophys Acta. 1983 Jun 9;757(3):302-5. doi: 10.1016/0304-4165(83)90055-7.
Previous experiments demonstrated the existence of at least two pools of secretory proteins in the exocrine pancreas. We have measured the specific activities of amylase released under resting conditions and of amylase in the zymogen granules. Specific activity of resting secretion was twice that found under stimulated conditions or in zymogen granules. Secretory proteins were pulse-labeled and amylase was measured after precipitation of the enzyme with glycogen. Pancreatic juice collected at 45-50 min post-pulse contained 10-25-times the amylase activity found in zymogen granules. These results confirm the existence of at least two distinct pools of secretory proteins in the exocrine pancreas and suggest the existence of an intracellular route of secretory proteins which would bypass the zymogen granule compartment.
先前的实验证明，外分泌胰腺中至少存在两池分泌蛋白。我们测定了在静息条件下释放的淀粉酶以及酶原颗粒中淀粉酶的比活性。静息分泌的比活性是刺激条件下或酶原颗粒中比活性的两倍。对分泌蛋白进行脉冲标记，并用糖原沉淀该酶后测定淀粉酶。脉冲后45 - 50分钟收集的胰液中淀粉酶活性是酶原颗粒中淀粉酶活性的10 - 25倍。这些结果证实了外分泌胰腺中至少存在两个不同的分泌蛋白池，并提示存在一条绕过酶原颗粒区室的分泌蛋白细胞内途径。
