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AuthorManko N.
AuthorStarykovych M.
AuthorBobak Y.
AuthorStoika R.
AuthorRichter V.
AuthorKoval O.
AuthorLavrik I.
AuthorHorák D.
AuthorSouchelnytskyi S.
AuthorKit Y.
Available date2020-04-05T10:53:21Z
Publication Date2019
Publication NameBiomedical Chromatography
ISSN2693879
URIhttp://dx.doi.org/10.1002/bmc.4647
URIhttp://hdl.handle.net/10576/13816
AbstractThe cytopoxic effect of RL2 lactaptin (the recombinant analog of proteolytic fragment of human kappa‐casein) toward tumor cells in vitro and in vivo presents it as a novel promising antitumor drug. The binding of any drug with serum proteins can affect their activity, distribution, rate of excretion and toxicity in the human body. Here, we studied the ability of RL2 to bind to various blood serum proteins. Using magnetic microparticles bearing by RL2 as an affinity matrix, in combination with mass spectrometry and western blot analysis, we found a number of blood serum proteins possessing affinity for RL2. Among them IgA, IgM and IgG subclasses of immunoglobulins, apolipoprotein A1 and various cortactin isoforms were identified. This data suggests that in the bloodstream RL2 lactaptin takes part in complicate protein–protein interactions, which can affect its activity.
SponsorThis work was financial supported by Volkswagen Foundation (grant # VW 90315).
Languageen
PublisherJohn Wiley and Sons Ltd
Subjecthuman blood serum proteins
Subjectidentification
Subjectmagnetic microparticles
Subjectmass spectrometry and western blotting
Subjectpurification
SubjectRL2 antitumor agent
TitleThe purification and identification of human blood serum proteins with affinity to the antitumor active RL2 lactaptin using magnetic microparticles
TypeArticle
Issue Number11
Volume Number33


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