You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Purification and Partial Characterization of Cysteine Proteinase from Spirometra mansoni Plerocercoids
Chul Yong Song and Cynthia L. Chappell
The Journal of Parasitology
Vol. 79, No. 4 (Aug., 1993), pp. 517-524
Stable URL: http://www.jstor.org/stable/3283376
Page Count: 8
You can always find the topics here!Topics: Plerocercoids, Parasitology, Sparganosis, Gels, Larvae, Molecular weight, Sodium, Enzymes, Collagens, Antibodies
Were these topics helpful?See something inaccurate? Let us know!
Select the topics that are inaccurate.
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Spirometra mansoni plerocercoids were dissected from the tissues of naturally infected snakes (Natrix trigrialateralia). Fresh plerocercoids were incubated in medium, and excretory-secretory products (E-S) were collected. In addition, soluble proteins from lyophilized plerocercoids (10 mg/ml) were extracted in 0.1 M sodium acetate. Proteinase activity was assayed with a synthetic fluorescent substrate, carbobenzoxy-phenylalanyl-arginyl-7-amino-4-trifluoromethylcoumarin. Proteinase was isolated from plerocercoid extract or E-S by diethylaminoethyl trisacryl M ion-exchange chromatography and thiolpropyl-Sepharose affinity chromatography. These separations resulted in a 12.2- (extract) and 15.6-fold (E-S) purification of proteinase. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified materials revealed a 28-kDa band, consistent with the apparent native molecular weight (gel filtration chromatography) of approximately 35 kDa. Proteinases purified from whole extracts and E-S were compared for various biochemical characteristics; inhibitor profiles indicated that activities from both sources are cysteine proteinases, they exhibited identical pH curves with optima at pH 5.5 and a 50% activity range at pH 4.7-8.0, they cleaved collagen chains to 3 identical products, and they showed only minor activity toward hemoglobin. Further, the proteinase purified from plerocercoids was utilized in immunoblots with sera from sparganosis patients. Antibody (IgG) from the infected patients, but not uninfected controls, recognized the cysteine proteinase, suggesting that this antigen may be useful in the serodiagnosis of Spirometra mansoni infection.
The Journal of Parasitology © 1993 The American Society of Parasitologists