title: Purification of granulocyte neutral protease from human blood and rheumatoid synovial fluid.
abstract: The neutral protease activity of human synovial fluid cells, like that of peripheral blood leucocytes, is located in a granule fraction. It can be solubilised by various agents but only 1 M neutral salts do so without inactivation. Salt-solubilised neutral protease has been purified (300 X) from synovial fluid cells; like preparations obtained in the same way (600 X purified) from peripheral blood leucocytes, it has a broad pH profile of activity (pH 7--10.5) and in this, as well as in substrate specificity and sensitivity to activators and inhibitors, it behaves as a serine-histidine type protease similar to elastase (EC 3.4.21.11). The product showed two major components on polyacrylamide gel electrophoresis. Collagenase or chymotrypsin-like activity were not detected.
mesh_terms: D001172:Arthritis, Rheumatoid / Q000201:enzymology*; D005966:Glucuronidase / Q000378:metabolism; D006098:Granulocytes / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D007962:Leukocytes / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000097:blood / Q000302:isolation & purification* / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology; D013582:Synovial Fluid / Q000201:enzymology*
chemical_list: D005966:Glucuronidase; D010447:Peptide Hydrolases