Open AccessISOLATION AND PURIFICATION OF PROTEIN THAT IS IMMUNOLOGICALLY SIMILAR TO HUMAN LACTOFERRIN
Author(s) -
Oksana Boîko,
А. И. Николаев,
Д. М. Козак,
Natalya Igorevna Gudinskaya,
Maxim Saharov,
Polina Gudinskaia,
Yuri Dotsenko
Publication year - 2021
Publication title -
archiv euromedica
Language(s) - English
Resource type - Journals
eISSN - 2199-885X
pISSN - 2193-3863
DOI - 10.35630/2199-885x/2021/11/2/2
Subject(s) - isoelectric point , lactoferrin , chromatography , chemistry , agarose , molecular mass , ammonium , electrophoresis , protein purification , isolation (microbiology) , ion exchange , biochemistry , microbiology and biotechnology , biology , ion , organic chemistry , enzyme
The study aimed at isolating a substance that is immunologically similar to human lactoferrin, hereinafter — microbial-derived lactoferrin (MdLF) isolated from K.pneumoniae liquid culture. Protein extraction started with isolation of ballast proteins in 2M ammonium sulphate (p.a.). Ion chromatography with cation-exchange agents was the basic method used for isolating MLF. Proteins from the isolated protein fractions were identified with AGID method. The isolated MLF is glucoprotein with the molecular mass of about 84,000, the agarose diffusion coefficient of 3.1 × 10–7 cm2 sec–1 and the relative electrophoretic mobility of 0.42. MLF is characterized by low hydrophobicity and elutes from phenylSepharose with 0.4 ammonium sulphate. Its isoelectric point equals to 9.2.