C-terminal truncation of bovine protein disulfide isomerase increases its activity.
Protein disulfide isomerase as usually purified by the method of Lambert and Freedman (Biochem. J., 1983, 213, 225-234) although appeared homogeneous by sodium dodecyl sulfate-polyacrylamide gel electrophoresis can be separated into two major components on a size-exclusion high performance liquid chromatography column or by polyacrylamide gel electrophoresis. These two components have the same N-terminal sequences but the C-terminal sequences are different, suggesting that one is the C-terminal slightly truncated protein. The shortened protein is more active in both the isomerase and the thiol-protein oxidoreductase activities.
Hu
C H
CH
National Laboratory of Biomacromolecules, Institute of Biophysics Academia Sinica, Beijing, China.
Tsou
C L
CL
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D007527:Isoenzymes; D007535:Isomerases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D019704:Protein Disulfide-Isomerases; D013438:Sulfhydryl Compounds / Q000378:metabolism
D007527:Isoenzymes; D013438:Sulfhydryl Compounds; D007535:Isomerases; D019704:Protein Disulfide-Isomerases