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Search Purification (Commentary)

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EC Number
Commentary
Reference
; the enzyme fraction is precipitated from kiwifruit extract by 60% saturation of ammonium sulfate. The precipitate is redissolved in 50 mM citrate buffer (pH 5.5) and dialyzed overnight against this buffer. The dialyzate is loaded into a DEAE-Sepharose Fast Flow column, which pre-equilibrated with the same buffer. The adsorbed fractions are eluted with 0.0-1 M linear gradient of sodium chloride in the buffer
Act d 1 is purified from kiwifruit extracts by covalent chromatography using activated thiopropyl sepharose 6B
actinidin can be separated into six proteases, named KP1, KP2, KP3, KP4, KP5 and KP6
Actinidin is purified from the soluble fraction of kiwi fruit by ion exchange chromatography on DE-52 and Mono-Q columns
ammonium sulfate precipitation and DEAE-Sephadex gel filtration
DEAE-Sephadex A-50 gel filtration and SP-Sephadex C-50 gel filtration
multiple forms
Results 1 - 7 of 7