Journal of Protein Chemistry

, Volume 13, Issue 2, pp 233–236 | Cite as

The essentiality of B chain in stabilizing the structure of the A chain in β1-bungarotoxin fromBungarus multicinctus venom

  • Long-sen Chang
  • Shinne-ren Lin
  • Chun-chang Chang
  • Chen-chung Yang


The dynamic of Trp residue inΒ1-bungarotoxin (gb1-Bgt), the A chain ofΒ1-Bgt and phospholipase A2 (PLA2) was assessed by fluorescence measurement. Acrylamide quenching studies showed that the exposure degree of the Trp in PLA2 is higher than the Trp inΒ1-Bgt. The Trp ofΒ1-Bgt had a higher accessibility for iodide, reflecting that the basic nature of the B chain might exert an attractive electrostatic force for iodide and increase the susceptibility of Trp in the A chain to iodide. Removal of the B chain ofΒ1-Bgt did not significantly affect the exposure degree of Trp in the A chain. Alternatively, the polarity of the environment around the Trp and the hydrophobic character of ANS and substrate binding sites in the separated A chain changed. Measurement of Trp fluorescence with increasing temperature showed that the stability of structure ofΒ1-Bgt was higher than those of the separated A chain and PLA2. These results suggest that the B chain might interact with the A chain and stabilize the conformation of the A chain inΒ1-Bgt.

Key words

Snake venom Trp fluorescence Β1-bungarotoxin role of the B chain 


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Copyright information

© Plenum Publishing Corporation 1994

Authors and Affiliations

  • Long-sen Chang
    • 1
  • Shinne-ren Lin
    • 1
  • Chun-chang Chang
    • 1
  • Chen-chung Yang
    • 2
  1. 1.Department of BiochemistryKaohsiung Medical CollegeKaohsiungTaiwan 807, Republic of China
  2. 2.Institute of Life SciencesNational Tsing Hua UniversityHsinchuTaiwan 304, Republic of China

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