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Abstract

  1. Top of page
  2. Abstract
  3. REFERENCES

The amino acid sequence of the α-subunit of taipoxin, an extremely potent presynaptic neurotoxin from the Australian snake taipan has been determined. The very basic protein, by itself a moderately neurotoxic phospholipase, consists of a single polypeptide chain of 119 amino acids. The main fragmentation of the reduced and S-carboxymethylated derivative was accomplished by cleavage with Staphylocoeus aureus V8 pro- tease and trypsin. Chymotryptic peptides and cyanogen bromide fragments were used to align and complete the sequence, which was determined by automated Edman degradation. The taipoxin γ-subunit is closely homologous to the other taipoxin subunits and to other elapid snake venom phospholipases A2.

Enzymes
 

Carboxypeptidase B (EC 3.4.17.2)

 

chymotrypsin (EC 3.4.21.1)

 

phospholipase A2 (EC 3.1.1.4)

 

Staphylococcus aureus V8 pro- tease (EC 3.4.21.19)

 

trypsin (EC 3.4.21.4)

REFERENCES

  1. Top of page
  2. Abstract
  3. REFERENCES
  • 1
    Fohlman, J., Eaker. D., Karlsson, E. & Thesleff, S. (1976) Eur. J. Biochem. 68, 457469.
  • 2
    Kamenskaya, M. A. & Thesleff, S. (1974) Acta Physiol. Scand. 90, 716724.
  • 3
    Chang, C. C. (1979) in Handbook of Experimental Pharmacology (Lec. C. Y., ed.) vol. 52, pp. 309359, Springer, Berlin, Heidelberg, New York .
  • 4
    Howard, B. D. & Gundersen, C. B. (1980) Annu. Rev. Pharmacol. Toxicol. 20, 307336.
  • 5
    Halpert, J. & Eaker. D. (1975) J. Biol. Chem. 250, 69906997.
  • 6
    Halpert, J. & Eaker. D. (1976) J. Biol. Chem. 251, 72437347.
  • 7
    Fohlman, J., Eaker. D., Dowdall, M. J., Lüllman-Rauch, R., Sjödin, T. & Leander, S. (1979) Eur. J. Biochem. 94, 531540.
  • 8
    Henden, R. A. & Fraenkel-Conrat, H. (1971) Proc. Natl Acad. Sci. U.S.A. 68, 15601563.
  • 9
    Rubsamen, K., Breithaupt, H. & Habermann. F. (1971) Naunyn-Schmiedeberg's Arch. Pharmacol. 270, 274288.
  • 10
    Wernicke, J. F., Vanker, A. D. & Howard, B. D. (1975) J. Neurochem. 25, 483496.
  • 11
    Eaker. D. (1978) in Versatility of Protiens (Li, C. H., ed.) pp. 413431. Academic Press, New York .
  • 12
    Halpert, J., Eaker, D. & Karlsson, E. (1976) FEBS Lett. 61, 7276.
  • 13
    Abe, T. Alemá, S. & Miledi, R. (1977) Eur. J. Biochem. 80, 112.
  • 14
    Jeng, T. W. & Fraenkel-Conrat, H. (1978) FEBS Lett. 87, 291296.
  • 15
    Fohlman, J., Lind, P. & Eaker, D. (1977) FEBS Lett. 84, 367371.
  • 16
    De Haas, G. H., Slotboom, A. J., Bonesn, P. P. M., van Deenen, L. L. M., Maroux, S., Puigserver, A. & Desnuelle, P. (1970) Biochim. Biophys. Acta, 221, 3153.
  • 17
    Puijk, W. C. Verheij, H. M. & de Haas, G. H. (1997) Biochim. Biophys. Acta, 492, 254259.
  • 18
    Lind, P. & Eaker, D. (1980) Eur. J. Biochem. 111, 403409.
  • 19
    Lind, P. & Eaker, D. (1981) Toxicon, 19, 1124.
  • 20
    Kondo, K., Narita, K. & Lec, C.-H. (1978) J. Biochem. (Tokyo) 83, 101115.
  • 21
    Eaker, D. (1975) in Peptides: Chemistry, Structure and Biology (Walter, R. & Meienhofer, J., eds) pp. 1730. Ann Arbor Science Publishers. Ann Arbor .
  • 22
    Porath, J. (1956) Biochim. Biophys. Acta, 22, 151175.
  • 23
    Iwanaga, S., Wallén, P., Gröndal, N. J., Henschen, A. & Blombäck, B. (1969) Eur. J. Biochem. 8, 189199.
  • 24
    Thomsen, J., Bucher, D., Brunfeldt, K., Nexo, E, & Olesen, H. (1976) Eur. J. Biochem. 69, 8796.