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Sepharose 4B-DNP-hexamethylenediamine as a sorbent for the chromatography of carboxylic proteinases

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Summary

1. The chromatography of the carboxylic proteinases porcine pepsin, aspergillopepsin A, and chymosin on the hydrophobic sorbent Sepharose 4B-DNP-hexamethylenediamine has been studied. It has been shown that the nature of the binding of the proteinases with the sorbent depends on the pH.

2. A shortening of the length of the carbohydrate chain of the ligand by four methylene units substantially weakens the interaction of pepsin with the sorbent.

3. With chymotrypsin and pepsin as examples, the possibility has been shown of using ionic effects for separating these enzymes.

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Authors
  1. V. P. Borovikova
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  2. N. N. Tarasova
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  3. G. N. Lavrenova
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  4. V. M. Stepanov
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Additional information

M. V. Lomonosov Moscow State University. Translated from Khimiya Prirodnykh Soedinenii, No. 2, pp. 191–199, March–April, 1979.

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Borovikova, V.P., Tarasova, N.N., Lavrenova, G.N. et al. Sepharose 4B-DNP-hexamethylenediamine as a sorbent for the chromatography of carboxylic proteinases. Chem Nat Compd 15, 161–168 (1979). https://doi.org/10.1007/BF00570789

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  • DOI: https://doi.org/10.1007/BF00570789

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