Proteases from purulent sputum. Purification and properties of the elastase and chymotrypsin-like enzymes

J Biol Chem. 1977 Mar 25;252(6):1917-26.

Abstract

A procedure is described for the purification of the elastase and chymotrypsin-like enzymes from purulent sputum. This procedure permitted the isolation of 132 mg and 120 mg of the elastase and chymotrypsin-like enzymes, respectively, from 230 g of purulent sputum. The elastase enzymes consist of a family of five isozymes, and at least three isozymes comprise the chymotrypsin-like enzyme system. The elastases proved to be immunologically identical with the corresponding enzyme of human leukocytes. These enzymes were characterized with respect to molecular weight, amino acid and carbohydrate composition, several kinetic parameters, and inhibition by various synthetic and natural inhibitors. The properties so found were comparable to those which had been previously reported by others for the elastase and chymotrypsin-like enzymes isolated directly from leukocytic granules.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acids / analysis
  • Chymotrypsin* / isolation & purification
  • Chymotrypsin* / metabolism
  • Emphysema / enzymology*
  • Hexosamines / analysis
  • Hexoses / analysis
  • Humans
  • Hydrogen-Ion Concentration
  • Immunodiffusion
  • Isoenzymes / isolation & purification
  • Isoenzymes / metabolism
  • Kinetics
  • Pancreatic Elastase* / isolation & purification
  • Pancreatic Elastase* / metabolism
  • Peptide Hydrolases* / isolation & purification
  • Peptide Hydrolases* / metabolism
  • Sialic Acids / analysis
  • Sputum / enzymology*
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Hexosamines
  • Hexoses
  • Isoenzymes
  • Sialic Acids
  • Peptide Hydrolases
  • Chymotrypsin
  • Pancreatic Elastase