Partial purification and characterization of cysteine proteinases from various developmental stages of Paragonimus westermani.
1. During development of Paragonimus westermani, larvae develop during migration within the host, and adult worms feed on pulmonary tissues, causing significant pathology in the mammalian host. In this report acidic extracts of various developmental stages (metacercariae and worms at one, two and three months of development) were examined for cysteine proteinase activity. 2. A soluble thiol-dependent proteinase activity with a native molecular weight of approximately 20,000 was isolated and partially purified. 3. The enzymes purified from the various developmental stages of the parasite had maximal activity at acidic pH and showed inhibitor susceptibilities similar to the vertebrate acidic cysteine proteinases. 4. Enzymatic activity was stable at pH 5.0 for at least two days when stored at 4 degrees C. 5. It is suggested that these enzymes may be involved in the nutrition of these parasites and/or during penetration and lysis of the tissues.
Song
C Y
CY
Department of Biology, Chung-Ang University, Seoul, Korea.
Dresden
M H
MH
D000818:Animals; D001391:Azo Compounds; D002850:Chromatography, Gel; D003094:Collagen; D004396:Coloring Agents; D003546:Cysteine Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010238:Paragonimus / Q000201:enzymology* / Q000254:growth & development; D011480:Protease Inhibitors / Q000494:pharmacology
D001391:Azo Compounds; D004396:Coloring Agents; D011480:Protease Inhibitors; C028470:Azocoll; D003094:Collagen; D003546:Cysteine Endopeptidases