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Purification and properties of the clotting enzyme from limulus lysate
Authors:James D. Sullivan  Stanley W. Watson
Affiliation:Woods Hole Oceanographic Institution, Woods Hole, Massachusetts 02543 USA
Abstract:
The clotting enzyme from Limulus lysate which is involved in the gelation reaction of lysate with endotoxin has been purified and some of its properties determined. It was isolated from endotoxin-treated lysate and purified by gel filtration, ion exchange chromatography, and disc gel electrophoresis. Reaction of clotting enzyme with lysate clottable protein produces a clot or gel such as occurs with the gelation of lysate by endotoxin. Purified clotting enzyme has an approximate molecular weight of 84,000 (subunit MW 43,000), is isoelectric at pH ca. 5.5, trypsin-like, heat labile and pH sensitive.
Keywords:CE  clotting enzyme  SDS  sodium dodecylsulfate  BANA  N-benzoyl-arginine naphthylamide  TAME  p-tosyl arginine methyl ester  pI  isoelectric point
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