Journal of comparative physiology

, Volume 127, Issue 4, pp 355–361 | Cite as

Comparison of digestive α-amylases from two species of spiders (Tegenaria atrica andCupiennius salei)

  • Thomas P. Mommsen
Article

Summary

  1. 1.

    Polyacrylamide gel electrophoreses of digestive fluids reveal the presence of two to three amylases (molecular mass about 58,000 Dalton) in the webbuilding spiderTegenaria atrica, and three enzymes (molecular mass about 63,000 Dalton) in the hunting spiderCupiennius salei. In either case, one amylase is largely predominant.

     
  2. 2.

    The dominating enzyme of each spider can be classified as an α-amylase (E.C.3.2.1.1) by the binding of and activation by chloride. TheK D is 1.6 mM for Cl at 30°C. Chloride concentrations below the optimum (<10 mM) have neither effect on pH-optimum nor onK m , but lowerV max .

     
  3. 3.

    Tegenaria andCupiennius amylases show identical behaviour with respect to all kinetic parameters studied, except for temperature dependence.

     
  4. 4.

    The Michaelis constants are around 4.5 mg/ml for soluble starch and for glycogen as substrates. Values forV max are slightly higher with soluble starch than with glycogen. Total activity is in the order of 50 to 75 nkat reducing groups per mg of protein of the unfractionated digestive fluid. pH-optima are near the pH of the digestive fluid (pH 7.4).

     
  5. 5.

    Discontinuous Arrhenius plots show that both amylases exist in at least two temperature-dependent conformational states. Activation enthalpy values are about 30% lower inTegenaria than inCupiennius amylases.

     
  6. 6.

    The amylases appear to be calcium-dependent enzymes which are non-competitively inhibited by Hg++ and Cu++.

     
  7. 7.

    Other anions activate the amylases similar to chloride, the effect decreasing with increasing iondiameter. Fluoride does neither activate nor inhibit.

     

Keywords

Enzyme Starch Enthalpy Fluoride Electrophoresis 

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Copyright information

© Springer-Verlag 1978

Authors and Affiliations

  • Thomas P. Mommsen
    • 1
  1. 1.Biological Institute IUniversity of FreiburgFreiburgFederal Republic of Germany

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