Simultaneous formation of native ribonuclease and proinsulin from their mixed S-sulfonated derivatives by protein disulfide isomerase.
Although the formation of native disulfide bonds of a protein from randomly linked disulfides by protein disulfide isomerase has been extensively studied, the possibility of simultaneous formation of the native proteins from a mixture has not been examined. It is shown in this paper that native ribonuclease and proinsulin can be nearly quantitatively formed by protein disulfide isomerase from a mixture of their S-sulfonated derivatives independent of the presence of each other.
Yu
X C
XC
National Laboratory of Biomacromolecules, Academia Sinica, Beijing, China.
Tsou
C L
CL
D004229:Dithiothreitol / Q000737:chemistry; D006801:Humans; D007535:Isomerases / Q000737:chemistry*; D011384:Proinsulin / Q000138:chemical synthesis*; D019704:Protein Disulfide-Isomerases; D012260:Ribonucleases / Q000138:chemical synthesis*; D013431:Sulfates / Q000737:chemistry*
D013431:Sulfates; D011384:Proinsulin; D012260:Ribonucleases; D007535:Isomerases; D019704:Protein Disulfide-Isomerases; D004229:Dithiothreitol