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[Sorbent for purification of diamine oxidase by the method of affinity chromatography].

Klimova Gi, Gromova Ln, Gorkin Vz

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Abstract

A substrate of diamine oxidase hexamethylene diamine was covalently bound through adipinic acid dihydrazide to Sepharose 4B in order to prepare a sorbent for the purification of diamine oxidase by means of biospecific (affinity) chromatography. A method was developed to purify diamine oxidase from pig kidney cortex using the sorbent. The method, comprising three steps, yielded enzyme preparations with specific activity 2 000-fold higher than that of kidney homogenate.

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A substrate of diamine oxidase hexamethylene diamine was covalently bound through adipinic acid dihydrazide to Sepharose 4B in order to prepare a sorbent for the purification of diamine oxidase by means of biospecific (affinity) chromatography. A method was developed to purify diamine oxidase from pig kidney cortex using the sorbent. The method, comprising three steps, yielded enzyme preparations with specific activity 2 000-fold higher than that of kidney homogenate.

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Available abstract

A substrate of diamine oxidase hexamethylene diamine was covalently bound through adipinic acid dihydrazide to Sepharose 4B in order to prepare a sorbent for the purification of diamine oxidase by means of biospecific (affinity) chromatography. A method was developed to purify diamine oxidase from pig kidney cortex using the sorbent. The method, comprising three steps, yielded enzyme preparations with specific activity 2 000-fold higher than that of kidney homogenate.

Key concepts: Diamine oxidase, Diamine, Sorbent, Amine oxidase (copper-containing), Affinity chromatography, Chemistry, Chromatography, Sepharose

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