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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. Binding of any drugs with serum proteins can affect their activity, distribution, rate of excretion, and toxicity of pharmaceutical agent in the human body. Here, we studied RL2 possibility to bind with different 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 different cortactin isoforms were identified. This data suggests that in bloodstream RL2 lactaptin takes part in complicate protein-protein interactions, which can affect its activity.
This article was published in the following journal.
Name: Biomedical chromatography : BMC
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Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.
All blood proteins except albumin ( = SERUM ALBUMIN, which is not a globulin) and FIBRINOGEN (which is not in the serum). The serum globulins are subdivided into ALPHA-GLOBULINS; BETA-GLOBULINS; and GAMMA-GLOBULINS on the basis of their electrophoretic mobilities. (From Dorland, 28th ed)
Procedures for identification and measurement of IMMUNOGLOBULINS in the blood that initiate lysis of bacteria.
Serum albumin from humans. It is an essential carrier of both endogenous substances, such as fatty acids and BILIRUBIN, and of XENOBITOICS in the blood.
The clear portion of BLOOD that is left after BLOOD COAGULATION to remove BLOOD CELLS and clotting proteins.
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