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- W3141557210 abstract "【Objective】Extraction and purification of angiotensin converting enzyme(ACE) was studied to provide technical support for its production and utilization.【Method】ACE crude extracts were purified by DEAE-Sepharose FF anion exchange and ultrafiltration after the fresh lung homogenate was centrifuged,precipitated and dialyzed using ammonium sulfate.ACE molecular weight,specific activity,purification fold and activity recovery were determined.【Result】Lung ACE obtained by SDS-PAGE showed ACE-pure and molecular mass was 182kDa.The ACE was purified to 357.31-fold with specific activity of 1.2476 U/mg and activity recovery of 12.28%.The Michaelis-constant of the ACE was 0.849 mmol/L and Vmaxwas 9.775nmol/min.【Conclusion】The ion exchange-ultrafiltration is an efficient purification method for lung ACE,as it can greatly shorten the separation and purification time,and get a higher purification fold and activity recovery." @default.
- W3141557210 created "2021-04-13" @default.
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- W3141557210 date "2014-01-01" @default.
- W3141557210 modified "2023-09-26" @default.
- W3141557210 title "Extraction and purification of angiotensin converting enzyme from fresh hog lung" @default.
- W3141557210 hasPublicationYear "2014" @default.
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