Hoppe-Seyler's Z. PhysioL Chem. Bd. 357, S. 1153 -1161, August 1976 Purification and Partial Characterization of Human Pancreatic Elastase Kjell OHLSSON and Ann-Sofie OLSSON Department of Clinical Chemistry and Surgery, University of Lund, Malmö General Hospital, Malmö, Sweden (Received 6 May 1976) Summary: 1) An elastolytic enzyme has been isolated from human pancreatic juice. The concentration of the enzyme was about 0.6 mg/m/ corresponding to about 10% of the protein concentration of the juice. 2) The purification procedure included chromatography on Sephadex G-25 followed by ion-exchange chromatography on SP-Sephadex C-50 at pH 6.0, affinity chromatography on TrasylolSepharose 4-B and a final ion-exchange chromatography on SP-Sephadex at pH 7.6. The yield was about 50%. 3) The elastase isolated was homogeneous in analytical disc electrophoresis and showed a single protein component with a molecular weight of 26 300 in dodecylsulfate-electrophoresis. There are similarities in the amino acid compositions of human and porcine pancreatic elastases. 4) The human enzyme has a lower activity on elastin than porcine elastase but similar activities on casein and fibrin. The Km value for Boc-Ala-ONp was 5.13 10~*M. The elastase isolated was 98% active, as judged from active site titration. 5) The results of immunodiffusion studies
hoppe-seyler's zeitschrift für physiologische chemie – de Gruyter
Published: Jan 1, 1976
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