Purification of alpha1-antitrypsin from plasma through thiol-disulfide interchange.

摘要: 1. Monomeric nu-chains were conjugated with CNBr-activated Sepharose 4B. The C-terminal cysteine of the nu-chain was converted to a mixed disulfide 3-carboxy-4-nitro-benzenethiol (Nbs) and used separate plasma proteins reactive thiol groups. proteins, alpha1-antitrypsin prealbumin have greatest affinity for interchange reaction disulfides. link between is sensitive excess Nbs, selectively cleaved in presence 5,5'-dithiobis(2-nitrobenzoate) (Nbs2) which accepts sulfhydryl group alpha1-antitrypsin. 2. A Simple method developed isolation human equally effective various inherited phenotypes from dog, baboon, monkey, Glutathione-Sepharose also successfully, but conjugate yielded less contaminated mercaptalbumin prealbumin. 3. harvested this procedure as Nbs. negative charge Nbs at pH 8.1 causes an increased electrophoretic mobility derivative. Mild reduction liberates returns normal. described can increase content fraction 5% total protein 95% within one day yield about 50%. This purification does not exert any detectable effect on microheterogeneity.