Komukai M, Kobayashi K, Horiuchi S
Comp Biochem Physiol B. 1986;85(1):55-9. doi: 10.1016/0305-0491(86)90220-8.
Degradation of muscle homogenate from the metamorphosing tadpole tail of bullfrog, Rana catesbeiana, was examined at acid and neutral pHs. More rapid and complete degradation was observed at acid pH. Proteinases working at acid pH were not inhibited by pepstatin but were inhibited by leupeptin. However, the inhibition by leupeptin was enhanced by pepstatin. These results show that lysosomal proteinases, a thiol proteinase(s) rather than cathepsin D, are involved in the degradation of tail muscle proteins.
对牛蛙(Rana catesbeiana)变态期蝌蚪尾巴肌肉匀浆在酸性和中性pH条件下的降解情况进行了研究。在酸性pH条件下观察到更快速且完全的降解。在酸性pH下起作用的蛋白酶不受胃蛋白酶抑制剂的抑制,但受亮抑蛋白酶肽的抑制。然而,胃蛋白酶抑制剂可增强亮抑蛋白酶肽的抑制作用。这些结果表明,溶酶体蛋白酶,即一种巯基蛋白酶而非组织蛋白酶D,参与了尾巴肌肉蛋白的降解。