Abstract:
:Proteins of Babesia equi piroplasms were characterized. The piroplasms of B. equi were purified by lysis of infected horse erythrocytes with N2 gas cavitation followed by separation in Percoll density-gradient centrifugation. The relative molecular weights (Mr) of major proteins separated by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis were 18, 28, 30, 41, 43, 54, 66.5, and 96 kDa. Immunoblot analysis using serum from an experimentally infected horse revealed six immunodominant proteins of 15, 18, 28, 30, 41, and 96 kDa. Two immunodominant proteins of 18 and 28 kDa were membrane-bound proteins as revealed by Triton X-114 phase partitioning.
journal_name
Parasitol Resjournal_title
Parasitology researchauthors
Ali S,Sugimoto C,Matsuda M,Sugiura T,Kanemaru T,Onuma M,Kamada Mdoi
10.1007/BF00932505subject
Has Abstractpub_date
1993-01-01 00:00:00pages
639-43issue
8eissn
0932-0113issn
1432-1955journal_volume
79pub_type
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