These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification and characterization of rat plasma alpha-1-antitrypsin.
    Author: Takahara H, Nakayama H, Sinohara H.
    Journal: J Biochem; 1980 Aug; 88(2):417-24. PubMed ID: 6968311.
    Abstract:
    alpha-1-Antitrypsin was purified from rat plasma using affinity chromatography on Cibacron Blue-agarose, ion-exchange chromatography on DE-52 (pH 8.5 and 6.0) and gel filtration on Sephadex G-150. The final preparation was homogeneous as judged by polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate, by immunoelectrophoresis and by analytical ultracentrifugation. It was composed of a single polypeptide chain whose molecular weight was estimated to be about 50,000 by sedimentation equilibrium analysis. Rat alpha-1-antitrypsin was shown to be a glycoprotein containing 3.3% glucosamine, 1.7% mannose, 1.0% galactose, and 4.2% sialic acid. The interaction of rat alpha-antitrypsin with bovine beta-trypsin was studied by protease activity assays and by gel electrophoresis in sodium dodecyl sulfate. Rat alpha-1-antitrypsin inhibited bovine beta-trypsin by forming a stable equimolar complex concomitant with the release of a peptide with a molecular weight of approx. 8,000.
    [Abstract] [Full Text] [Related] [New Search]