Biochemical properties of an intracellular serpin from Echinococcus multilocularis.
A serpin of the intracellular type from the tapeworm Echinococcus multilocularis was expressed in Escherichia coli, purified by ion exchange chromatography and tested for inhibitory activity against several proteinases. The recombinant protein, which after transcriptional induction, represents about 20 % of total cellular protein, is biochemically active and inhibits trypsin and the trypsin-like plasmin as well as pig pancreatic and human neutrophil elastase. Implications regarding its biochemistry and biological function are discussed.
Merckelbach
Armin
A
Department of Tropical Hygiene and Public Health, University Clinic Heidelberg, Im Neuenheimer Feld 324, 69 120, Heidelberg, Germany. om6@ix.urz.uni-heidelberg.de
Ruppel
Andreas
A
D000818:Animals; D048210:Echinococcus multilocularis / Q000201:enzymology* / Q000235:genetics; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D019272:Leukocyte Elastase / Q000037:antagonists & inhibitors; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D015843:Serpins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000378:metabolism
D015801:Helminth Proteins; D011994:Recombinant Proteins; D015843:Serpins; D014361:Trypsin Inhibitors; D010196:Pancreatic Elastase; D019272:Leukocyte Elastase