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Purification and chemical characterization of α‐fetoprotein from rat and mouse
Author(s) -
Watabe Hiroyuki
Publication year - 1974
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910130313
Subject(s) - isoelectric focusing , isoelectric point , sodium dodecyl sulfate , gel electrophoresis , microbiology and biotechnology , electrophoresis , homogeneous , chemistry , biochemistry , alpha fetoprotein , antibody , molecular mass , biology , chromatography , immunology , enzyme , genetics , physics , hepatocellular carcinoma , thermodynamics
Abstract Alpha‐fetoprotein of the rat was immunochemically purified and characterized. Mouse α‐fetoprotein, which cross‐reacts with antibodies to rat α‐fetoprotein, was also purified. Rat α‐fetoprotein was heterogeneous in disc electrophoresis and isoelectric focusing and had two different isoelectric points at pH 4.76 and 5.05. Mouse α‐fetoprotein was homogeneous when analyzed similarly. The molecular weight of both rat and mouse α‐fetoprotein was 70,000 as determined by gel electrophoresis in the presence of sodium dodecyl sulfate. The two specimens revealed a close similarity also in some other physicochemical, chemical and immunological properties.