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.
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Literature cited
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Additional information
All-Union Scientific-Research Institute of the Genetics and Breeding of Industrial Microorganisms, Moscow. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 75–80, January–February, 1976.
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Lyubinskaya, L.A., Lastovetskaya, L.V., Shekhvatova, G.V. et al. Determination of the activity of neutral proteinases with respect to the homogeneous substrate 2,4-dinitrophenylglycylglycyl-L-valyl-L-arginine. Chem Nat Compd 12, 63–67 (1976). https://doi.org/10.1007/BF00570185
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DOI: https://doi.org/10.1007/BF00570185