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Studies on the active center of pancreatic amylase

II. Small angle X-ray scattering investigations

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Summary

  1. 1.

    The radius of gyration of α-amylase is 26.9 Å, as found by means of small angle X-ray scattering. This value decreases by 0.5 Å if amylase binds three moles ofβ-cyclodextrin per mole enzyme.

  2. 2.

    In case of partial saturation, the solution contains only saturated amylase-cyclodextrin complexes (amylase/cyclodextrin molar ratio 1:3) and amylase molecules free of cyclodextrin. The binding of β-cyclodextrin follows the all-or-none mechanism.

  3. 3.

    The specifically bound β-cyclodextrin molecules are accommodated in a trough of the amylase molecule. The plane of bound cyclodextrin is perpendicular to the longitudinal axis of the trough. It is suggested that the helical substrate, amylose, binds in this trough, too.

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References

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Author notes

  1. Pál Elödi

    Present address: Department of Biochemistry, University Medical School, P.O.B. 6, H-4012, Debrecen, Hungary

Authors and Affiliations

  1. Enzymology Department, Institute of Biochemistry, Hungarian Academy of Sciences, P.O.B. 7, H-1502, Budapest, Hungary

    István Simon, Susan Móra & Pál Elödi

Authors
  1. István Simon
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  2. Susan Móra
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  3. Pál Elödi
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Simon, I., Móra, S. & Elödi, P. Studies on the active center of pancreatic amylase. Mol Cell Biochem 4, 211–216 (1974). https://doi.org/10.1007/BF01731483

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  • DOI: https://doi.org/10.1007/BF01731483

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