Reduction and Reoxidation of the Disulphide Bonds of Pepsinogen.

摘要

Both native and re-oxidized pepsinogen were subjected to starch-gel electrophoresis for 4 h at 4 degrees using a 7.0 mM tris-citrate buffer, pH 8.4, with subsequent development of the gel slab by amino black dye. The former showed one well-defined zone with two minor components which migrated behind the major zone. Re-oxidized material gave the same major band with a broad ill-defined trailing region, the front of which moved at a rate intermediate to the two lesser components found in the native protein sample. These experiments indicate that the tertiary and most of the secondary structure of pepsinogen can be disrupted without greatly affecting the ability of polypeptide chain to recover some of its structure and possibly as a consequence, some of its activity. At present, however, it would be premature to assert that the recovered active molecule is identical in all respects to native pepsinogen. (Author)