Literature DB >> 10940823

Isolation and properties of human alpha-fetoprotein from HepG2 cell cultures.

H F Deutsch1, N Taniguchi, M A Evenson.   

Abstract

A relatively rapid 3-step fractionation method has been developed for the isolation of human alpha-fetoprotein from culture fluids of HepG2 cells applicable to large volumes. The protein exists as a complex with lipids or lipoproteins but an ethanol precipitation step is effective in separating it. Yields of 50-60% can be obtained from culture fluid containing 30-40 microg/ml. A minor fraction that appears to be a proteolytic product of the AFP is present in the final product. Copyright 2000 S. Karger AG, Basel.

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Year:  2000        PMID: 10940823     DOI: 10.1159/000030132

Source DB:  PubMed          Journal:  Tumour Biol        ISSN: 1010-4283


  1 in total

1.  Ipomoeassin-F disrupts multiple aspects of secretory protein biogenesis.

Authors:  Peristera Roboti; Sarah O'Keefe; Kwabena B Duah; Wei Q Shi; Stephen High
Journal:  Sci Rep       Date:  2021-06-02       Impact factor: 4.379

  1 in total

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