Literature DB >> 1694995

Isolation of nine human plasma proteinase inhibitors by sequential affinity chromatography.

A Dubin1, J Potempa, J Travis.   

Abstract

Purification of nine plasma proteinase inhibitors and one zymogen from a single batch of human plasma, using affinity chromatography has been accomplished. Those isolated were plasminogen (lysine-Sepharose), alpha-2-antiplasmin (plasminogen-Sepharose), high and low molecular weight kininogens (CM-papain-Sepharose), alpha-2-macroglobulin (Zn++ chelate-Sepharose), alpha-1-proteinase inhibitor, alpha-1-antichymotrypsin, Cl-inhibitor, inter-alpha-trypsin inhibitor (Blue-Sepharose) and antithrombin III (heparin-Sepharose). Alpha-2-macroglobulin and alpha-1-proteinase inhibitor required gel filtration as additional purification steps. Each protein was recovered in both high yield and purity.

Entities:  

Mesh:

Substances:

Year:  1990        PMID: 1694995     DOI: 10.1080/00327489008050177

Source DB:  PubMed          Journal:  Prep Biochem        ISSN: 0032-7484


  3 in total

1.  The primary elastase inhibitor (elastasin) and trypsin inhibitor (contrapsin) in the goat are serpins related to human alpha 1-anti-chymotrypsin.

Authors:  J Potempa; J J Enghild; J Travis
Journal:  Biochem J       Date:  1995-02-15       Impact factor: 3.857

Review 2.  Methods of Purification and Application Procedures of Alpha1 Antitrypsin: A Long-Lasting History.

Authors:  Simona Viglio; Paolo Iadarola; Maura D'Amato; Jan Stolk
Journal:  Molecules       Date:  2020-09-02       Impact factor: 4.411

3.  Reply to Harwood et al.: Alternative functional conformations of native human α2-macroglobulin.

Authors:  Daniel Luque; Theodoros Goulas; Carlos P Mata; Soraia R Mendes; F Xavier Gomis-Rüth; José R Castón
Journal:  Proc Natl Acad Sci U S A       Date:  2022-08-16       Impact factor: 12.779

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.