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  • Title: Isolation and characterization of porcine leukocyte elastase. Leukocyte elastase-inhibitor complexes in porcine blood, II.
    Author: Geiger R, Junk A, Jochum M.
    Journal: J Clin Chem Clin Biochem; 1985 Dec; 23(12):821-8. PubMed ID: 3854325.
    Abstract:
    Porcine leukocyte elastase was purified from granulocytes by chelating chromatography on copper chelate Sepharose and by ion exchange chromatography on CM-Sepharose. Thus an enzyme preparation with a specific activity (substrate: MeOSuc(Ala)2ProValNan) of 89.3 U/mg protein was obtained. Dodecyl sulphate gel electrophoresis revealed one protein band corresponding to a molecular mass of 27 kDa. The amino acid composition was determined and isoleucine was identified as the only N-terminal amino acid residue. The bimolecular velocity constant for the inhibition by diisopropyl fluorophosphate was determined as 2000 1 . mol-1 . min-1. The dissociation constants, Ki, of the complexes of porcine leukocyte elastase with various inhibitors were calculated. The kinetic constants for the elastase-catalysed hydrolysis of MeOSuc(Ala)2ProValNan, Suc(Ala)2ValNan and Suc(Ala)3Nan were determined, as well as the kinetic constants of the inactivation of leukocyte elastase by active site mapping reagents. Detergents such as Triton X-100, Tween 20 and Brij 35, as well as porcine serum albumin, activated the porcine leukocyte elastase preparation.
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