Chemistry of Natural Compounds

, Volume 12, Issue 1, pp 63–67 | Cite as

Determination of the activity of neutral proteinases with respect to the homogeneous substrate 2,4-dinitrophenylglycylglycyl-L-valyl-L-arginine

  • L. A. Lyubinskaya
  • L. V. Lastovetskaya
  • G. V. Shekhvatova
  • T. I. Vaganova
  • V. M. Stepanov
Article
  • 17 Downloads

Summary

1. A chromogenic specific substrate for neutral proteinases — 2,4-dinitrophenylglycylglycyl-L-valyl-L-arginine — has been synthesized.

2. A method has been developed for determining the activity of neutral proteinases in enzyme preparations with the use of this substrate which is based on the spectrophotometric determination of DNP-glycylglycine formed on the cleavage of the glycyl-valyl bond in the substrate.

3. The applicability of the method to the determination of thermolysin and of the neutral proteinase fromBacillus subtilis has been shown.

Keywords

Methyl Ester Enzyme Preparation Cotton Plant DMFA Neutral Proteinase 

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Literature cited

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Copyright information

© Plenum Publishing Corporation 1977

Authors and Affiliations

  • L. A. Lyubinskaya
  • L. V. Lastovetskaya
  • G. V. Shekhvatova
  • T. I. Vaganova
  • V. M. Stepanov

There are no affiliations available

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