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. 1990 Jul;58(7):2071–2075. doi: 10.1128/iai.58.7.2071-2075.1990

Identification of isolate-specific sporozoite proteins of Cryptosporidium parvum by two-dimensional gel electrophoresis.

J R Mead 1, R C Humphreys 1, D W Sammons 1, C R Sterling 1
PMCID: PMC258778  PMID: 2365452

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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