Isolation of low-molecular albumins of 2S fraction from soybean (Glycine max (L.) Merrill).
Author(s) -
Mariola Galbas,
Filip Porzucek,
Anna Woźniak,
Ryszard Słomski,
Marek Selwet
Publication year - 2013
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.2013_1958
Subject(s) - isoelectric point , molecular mass , glycine , hela , chemistry , biochemistry , peptide , albumin , isolation (microbiology) , isoelectric focusing , chromatography , cell , biology , amino acid , enzyme , bioinformatics
Numerous studies have shown that consumption of soybean products decrease the risk of cancers in humans. Experiments at the molecular level have demonstrated that in most cases proteins and peptides are responsible for the anticancer properties of soybeen. Special attention should be paid to lunasin - a peptide described for the first time 16 years ago. Due to its structure it causes i.a., inhibition of cancer cell proliferation. A novel procedure for the isolation and purification of low-molecular-mass 2S soybean albumin protein is described in the present paper. A fraction of four peptides one of them corresponding to molecular mass and isoelectric point characteristic for lunasin. The obtained peptides decreased on the rate of HeLa cell proliferation.
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