Research Article

Rapid Purification and Procoagulant and Platelet Aggregating Activities of Rhombeobin: A Thrombin-Like/Gyroxin-Like Enzyme from Lachesis muta rhombeata Snake Venom

Table 2

Measured molecular masses and deduced amino acid sequences obtained by ESI-Q-Tof-MS/MS based on the alkylated SV-8 peptides of Rhombeobin.

PeptidePositionAmino acid sequenceMeasured mass (Da)

S-11–11VI/LGGDECNINE1218.5202
S-212–36HRFI/LVAI/LYDGI/LSGTFI/LCGGTI/LI/LNQE2780.3842
S-337–48WVI/LTAAHCDSE1287.5534
S-466–72QTRYPKE 920.4763
S-573–82KYFFRCPNKKNDE1744.8213
S-6134–150TI/LPDVPHCANI/LNI/LI/LDYE1982.8704
S-7151–174VCRAAYAGI/LPATSRVI/LCAGVI/LE2333.1693

The peptides were separated by RP-HPLC and were sequenced by mass spectrometry. C = alkylated cysteine; glutamic acid residues shown in bold were deduced on the cleavage Streptoccocus aureus SV-8. All molecular masses are reported as monoisotopic.