Serotriflin, a CRISP family protein with binding affinity for small serum protein-2 in snake serum

Narumi Aoki, Akie Sakiyama, Kimiko Kuroki, Katsumi Maenaka, Daisuke Kohda, Masanobu Deshimaru, Shigeyuki Terada

    Research output: Contribution to journalArticle

    16 Citations (Scopus)

    Abstract

    Habu (Trimeresurus flavoviridis) serum contains 3 small serum proteins (SSP-1, SSP-2, and SSP-3) with molecular masses of 6.5 to 10 kDa. Gel filtration analysis showed that all the SSPs exist in high molecular mass forms of approximately 60 kDa in the serum. Ultrafiltration of Habu serum showed that SSPs dissociated from the complex below a pH of 4. An SSP-binding protein was purified from Habu serum by gel filtration, ion exchange, and reverse-phase HPLC. N-terminal sequencing yielded a 39-amino acid sequence, similar to the N-terminal region of triflin, which is a snake venom-derived Ca2+ channel blocker that suppresses smooth muscle contraction. The amino acid sequence of this protein, termed serotriflin, was established by peptide analysis and cDNA cloning. Serotriflin is a glycosylated protein and consists of 221 amino acids. Among the 3 SSPs, only SSP-2 formed a noncovalent complex with serotriflin. It was bound to triflin and serotriflin with high affinity, as evidenced by surface plasmon resonance. SSP-2 is considered to be a protein that prevents self injury by accidental leaking of venom into the blood.

    Original languageEnglish
    Pages (from-to)621-628
    Number of pages8
    JournalBiochimica et Biophysica Acta - Proteins and Proteomics
    Volume1784
    Issue number4
    DOIs
    Publication statusPublished - Apr 1 2008

    All Science Journal Classification (ASJC) codes

    • Analytical Chemistry
    • Biophysics
    • Biochemistry
    • Molecular Biology

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