Identification of isolate-specific sporozoite proteins of Cryptosporidium parvum by two-dimensional gel electrophoresis.
AUTOR(ES)
Mead, J R
RESUMO
Five isolates of Cryptosporidium parvum collected from human, horse, and calf sources were compared for differences in sporozoite protein patterns by using two-dimensional gel electrophoresis. Silver-stained two-dimensional gels contained over 300 protein spots from detergent-solubilized sporozoites. A distinguishing 106-kilodalton peptide that shifted in isoelectric point was detected in four of the five isolates. Computerized two-dimensional gel analysis was performed to obtain objective quantitation of the pI shift. Three of these four isolates could be differentiated from one other by the pI shift in this peptide. The fifth isolate was distinguished by the absence of the 106-kilodalton peptide and the presence of a 40-kilodalton peptide that was not observed in any other isolate.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=258778Documentos Relacionados
- Degradation of cellular proteins during poliovirus infection: studies by two-dimensional gel electrophoresis.
- Identification of protein binding sites in genomic DNA by two-dimensional gel electrophoresis.
- Influenza virus proteins: identity, synthesis, and modification analyzed by two-dimensional gel electrophoresis.
- Characterization and identification of early proteins in Chlamydia trachomatis serovar L2 by two-dimensional gel electrophoresis.
- Analysis of secondary modifications of mouse mammary tumor virus proteins by two-dimensional gel electrophoresis.