Refolding of serine proteinases
โ
Albert Light; Chester T. Duda; Thomas W. Odorzynski; William G. I. Moore
๐
Article
๐
1986
๐
John Wiley and Sons
๐
English
โ 389 KB
Bovine trypsinogen and chymotrypsinogen were successfully refolded as the mixed disulfide of glutathione using cysteine as the disulfide interchange catalyst. The native structures were regenerated with yields of 40%-50% at pH 8.6 and 4"C, and the half-time for the refolding was approximately 60-75