Journal: Toxins

Article Title: Comparative Study of Biological Activities of Venom from Colubrid Snakes Rhabdophis tigrinus (Yamakagashi) and Rhabdophis lateralis

doi: 10.3390/toxins9110373

Figure Lengend Snippet: Proteolytic activity of venom fractions on fluorescence-quenching substrate for matrix metalloproteinases.

Article Snippet: The fluorescence-quenching substrate for matrix metalloproteinases; NFF-2 (MCA–Arg–Pro–Lys–Pro–Tyr–Ala–Nva–Trp–Met–Lys(Dnp)–NH 2 ), NFF-3 (MCA–Arg–Pro–Lys–Pro–Val–Glu–Nva–Trp–Arg–Lys(Dnp)–NH 2 ), 3163v (MCA–Pro–Leu–Gly–Leu–Dpa–Ala–Arg–NH 2 ), and the reference compound MOCAc–Pro–Leu–Gly were purchased from Peptide Institute, Inc. (Osaka, Japan). α-Cyano-4-hydroxycinnamic acid (HCCA), a matrix substance for MALDI-TOF MS and peptide calibration standard were obtained from Bruker Daltonics (Yokohama, Japan).

Techniques: Activity Assay, Fluorescence