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Characterization of a Hemoglobin-like Protein from Adult Haemonchus contortus
Raymond H. Fetterer, Dolores E. Hill and Marcia L. Rhoads
The Journal of Parasitology
Vol. 85, No. 2 (Apr., 1999), pp. 295-300
Stable URL: http://www.jstor.org/stable/3285637
Page Count: 6
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A hemoglobin-like protein was purified from supernatants of adult Haemonchus contortus extracts by high-pressure liquid chromatography. The purified protein had an Mr of 33 kDa as determined by size-exclusion chromatography under non-denaturing conditions and an Mr of 19 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting the hemoglobin may exist as a dimer. The sequences of 3 peptides resulting from proteolytic digest of the purified protein were determined and demonstrated greater than 50% identity to the globin from Trichostrongylus colubriformis. Adult H. contortus incubated overnight in [3H]leucine, incorporated radioactivity into a peak that coeluted with parasite hemoglobin, indicating the adults synthesize hemoglobin in vitro. The L3-stage lacked hemoglobin, but the L4-stage contained a hemoglobin with an Mr of 19.6 kDa.
The Journal of Parasitology © 1999 The American Society of Parasitologists