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.
Purification and characterization of prolixin S (nitrophorin 2), the salivary anticoagulant of the blood-sucking bug Rhodnius prolixus
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J M C Ribeiro, M Schneider, J A Guimarães; Purification and characterization of prolixin S (nitrophorin 2), the salivary anticoagulant of the blood-sucking bug Rhodnius prolixus. Biochem J 15 May 1995; 308 (1): 243–249. doi: https://doi.org/10.1042/bj3080243
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