1988 Volume 44 Issue 8 Pages 374-378
The fine structure of Chinon fibers treated with some proteases was examined. Under optical microscope, the cross sections of Chinon fiber stained with C. I. Acid Red 249 revealed that Pronase P (Pro) and Proteoliquifase (Plf) both eliminated the protein component of the fiber progressively from its surface region to the center, while the distribution of protein was apparently uniform in the intact fibers. On the other hand, Papain C-400 (Pap) seemed to digest the protein uniformly under the same conditions. Under transmission electron microscope, the cross sections stained with osmium oxide revealed that the protei component distributed uniformly in Chinon fiber as fine units of less than 200 Å in diameter. Furthermore, it was observed that Pro and Plf decreased not only the diameter but also the density of the protein units according to the progress of the proteolysis, while Pap seemed to decrease only the density but not the diameter of the components. Thus, introduction of certain micro-void spaces was expected at the positions corresponding to those stainable by osmium oxide before but unstainable after the proteolysis. However, direct observation by a scanning electron microscope was unable to detect the micro-void spaces probably because of their dimension out of the resolution.