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

Table 1

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

Peptide	Position	Amino acid sequence	Measured mass (Da)
T-1	1–13	VI/LGGDECNI/LNEHR	1497.6263
T-2	60–71	VPNEDEQTKYPK	1474.7011
T-3	72–80	EKYFFRCPNKK	1463.7229
T-4	85–93	WDKDI/LMI/LI/LR	1188.6088
T-5	94–121	I/LDSPVSNSEHI/LAPI/LSI/LPSNPPSVGSV𝐶 R	2915.3930
T-6	122–132	I/LMGWGQTI/LTSPK	1317.6720
T-7	160–183	VI/LCAGVI/LEGGI/LDTCNR	1732.7533
T-8	184–217	DSGGPI/LI/LCNGQFQGI/LASWGPDPCAQPDKPAVYTK	3630.5924
T-9	218–239	VFDYTDWI/LQNI/LI/LAGNTDATCPP	2496.0740

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