Chemistry of Natural Compounds

, Volume 11, Issue 5, pp 670–672 | Cite as

Isolation and study of the protease-inhibitor system of wheat grain

  • O. V. Fursov


A modified method for obtaining a protease and its natural protein inhibitor from the endosperm of wheat grain is proposed. The enzyme is purified by additional precipitation of part of the ballast proteins with ammonium sulfate, and the inhibitor by two successive precipitations of the bulk of the inactive protein with the aid of TCA of different concentrations. The specific activity of the protease increases by a factor of 5–6, and the activity of the inhibitor by a factor of 3–4. Two active isoenzymes of protease have been found in each of the varieties of wheat investigated by disk eletrophoresis.


Ammonium Sulfate Papain Inhibitor System Inactive Protein Hard Wheat 


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Copyright information

© Plenum Publishing Corporation 1976

Authors and Affiliations

  • O. V. Fursov

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