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Isolation and purification of biopolymers by affinity chromatography. VI. Preparation and properties of an affinity adsorbent with a polysaccharide spacer for the purification of proteolytic enzymes

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Abstract

A new affinity sorbent has been synthesized — soybean trypsin inhibitor (STI)-amylopectin-hydrazidosuccinyl-Sepharose — and its properties have been studied in comparison with those of an analogous adsorbent without the spacer STI-Sepharose. The STI-amylopectin-hydrazidosuccinyl-Sepharose adsorbent has been used for the purification of trypsin from porcine pancreas and of callicrein from human blood plasma.

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Authors
  1. V. Kh. Mitina
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  2. R. I. Yakubovskaya
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  3. B. A. Klyashchitskii
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  4. F. M. Shemyakin
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Additional information

For Communication V, see [1].

Institute of Biological and Medicinal Chemistry, Academy of Medical Sciences of the USSR, Moscow. I. M. Sechenov First Moscow Medical Institute. Translated from Khimiya Prirodnykh Soedinenii, No. 4, pp. 556–560, July–August, 1980.

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Mitina, V.K., Yakubovskaya, R.I., Klyashchitskii, B.A. et al. Isolation and purification of biopolymers by affinity chromatography. VI. Preparation and properties of an affinity adsorbent with a polysaccharide spacer for the purification of proteolytic enzymes. Chem Nat Compd 16, 405–408 (1980). https://doi.org/10.1007/BF00568379

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  • DOI: https://doi.org/10.1007/BF00568379

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