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Characterization and identification of red diamond back rattlesnake venom proteins
Author(s) -
Joshi Amod N,
Krishna Sharath,
Grunwald William C,
Cool David R
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.1122.5
Subject(s) - venom , snake venom , trypsin , chemistry , biochemistry , elapidae , biology , enzyme
Snake venom, although feared for its life threatening effect, is a source of potential bioactive molecules of therapeutic value. While cardiotoxins, myotoxins and neurotoxins constitute the harmful fraction of snake venom; disintegrins and metalloproteinase's are proposed to have anti‐cancer properties. The primary objective of this study is to fractionate, characterize and identify snake venom proteins/peptides. The components of crude venom of Red DiamondBack rattlesnake (RDB) were separated by gel electrophoresis and digested with trypsin. The mass profiling of the digested fractions was carried out using MALDI‐TOF MS followed by identification of proteins using the in‐house MASCOT server. One protein from RDB venom was identified from this initial round of analysis, i.e., the enzyme hemorrhagic metalloproteinase (HT‐2). Our search results showed that HT‐2 had protein scores above the threshold with an indication of 31 percent identity (p<0.05). In conclusion, this approach provides the first round of identification prior to assessing the functionality of individual snake venom proteins as anti‐cancer agents. This work is supported by an NIH grant (1P20MD003350‐04) to Central State University, Ohio.