Literature DB >> 17040689

Biology of giant proteins of Plasmodium: resolution on polyacrylamide-agarose composite gels.

J Wiesner1, D Mattei, A Scherf, M Lanzer.   

Abstract

The malaria parasite Plasmodium falciparum that infects humans encodes several extremely large proteins with molecular masses in the hundreds of thousands to megadalton range. Studies on the structure, function and antigenicity of these ;giant proteins' are hindered by the inability to resolve them effectively in conventional polyacrylamide gels. In this report, Jochen Wiesner, Denise Mattei, Artur Scherf and Michael Lanzer describe a convenient gel system, based on a composite polyacrylamide-agarose matrix, which facilitates analysis of giant proteins.

Entities:  

Year:  1998        PMID: 17040689     DOI: 10.1016/s0169-4758(97)01155-1

Source DB:  PubMed          Journal:  Parasitol Today        ISSN: 0169-4758


  3 in total

1.  Plasmodium falciparum domain mediating adhesion to chondroitin sulfate A: a receptor for human placental infection.

Authors:  P A Buffet; B Gamain; C Scheidig; D Baruch; J D Smith; R Hernandez-Rivas; B Pouvelle; S Oishi; N Fujii; T Fusai; D Parzy; L H Miller; J Gysin; A Scherf
Journal:  Proc Natl Acad Sci U S A       Date:  1999-10-26       Impact factor: 11.205

2.  Interaction of the exported malaria protein Pf332 with the red blood cell membrane skeleton.

Authors:  Karena L Waller; Lisa M Stubberfield; Valentina Dubljevic; Donna W Buckingham; Narla Mohandas; Ross L Coppel; Brian M Cooke
Journal:  Biochim Biophys Acta       Date:  2010-02-02

3.  Antibody responses to the repetitive Plasmodium falciparum antigen Pf332 in humans naturally primed to the parasite.

Authors:  N Ahlborg; D Haddad; A B Siddique; C Roussilhon; C Rogier; J F Trape; M Troye-Blomberg; K Berzins
Journal:  Clin Exp Immunol       Date:  2002-08       Impact factor: 4.330

  3 in total

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