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. 1995 May 15;308(Pt 1):243–249. doi: 10.1042/bj3080243

Purification and characterization of prolixin S (nitrophorin 2), the salivary anticoagulant of the blood-sucking bug Rhodnius prolixus.

J M Ribeiro 1, M Schneider 1, J A Guimarães 1
PMCID: PMC1136869  PMID: 7755571

Abstract

The salivary anticoagulant of the blood-sucking bug Rhodnius prolixus was purified to homogeneity using a protocol consisting of weak cation-exchange, DEAE, hydrophobic-interaction and octadecyl reverse-phase chromatography, yielding a protein with the same N-terminal sequence as nitrophorin 2, one of the four NO haem protein carriers present in the salivary glands of Rhodnius with a molecular mass of 19689 Da [D. Champagne, R.H. Nussenzveig and J.M.C. Ribeiro, (1995) J. Biol. Chem. 270, in the press]. To exclude the possibility of the nitrophorin being a contaminant, another chromatographic protocol was performed, consisting of chromatofocusing followed by strong-cation-exchange chromatography. Again the anticoagulant was eluted with nitrophorin 2. Nitrophorin 2 inhibits coagulation Factor VIII-mediated activation of Factor X and accounts for all the anti-clotting activity observed in Rhodnius salivary glands.

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Selected References

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