Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Comparison of interaction between ceruloplasmin and lactoferrin/transferrin : to bind or not to bind. / Sokolov, A. V.; Voynova, I. V.; Kostevich, V. A.; Vlasenko, A. Yu; Zakharova, E. T.; Vasilyev, V. B.
в: Biochemistry (Moscow), Том 82, № 9, 01.09.2017, стр. 1073-1078.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Comparison of interaction between ceruloplasmin and lactoferrin/transferrin
T2 - to bind or not to bind
AU - Sokolov, A. V.
AU - Voynova, I. V.
AU - Kostevich, V. A.
AU - Vlasenko, A. Yu
AU - Zakharova, E. T.
AU - Vasilyev, V. B.
PY - 2017/9/1
Y1 - 2017/9/1
N2 - The year 2016 marked the 50th anniversary of the discovery by S. Osaki who first showed that ceruloplasmin (CP, ferro:O2-oxidoreductase or ferroxidase) is capable of oxidizing Fe(II) to Fe(III) and favors the incorporation of the latter into transferrin (TF). However, much debate remains in the literature concerning the existence of a complex between the enzyme oxidizing iron and the protein facilitating its transport in plasma. We studied CP in exocrine fluids and demonstrated its high-affinity interaction with transferrin found in breast milk and in lacrimal fluid, i.e. with lactoferrin (LF). Here we present data obtained by comparing the interaction of CP with LF and TF using surface plasmon resonance and Hummel–Dreyer chromatography. Binding of apo-LF within the range of concentrations 1.6-51.3 μM with CP immobilized on a CM5-chip is characterized by KD = 1.07 μM. Under similar conditions, the KD for apo-TF was measured and appeared to be higher than 51.3 μM. Hummel–Dreyer chromatography of CP with 51 μM apo-LF/apo-TF in the effluent demonstrated the absence of interaction between apo-TF and CP in solution, contrary to efficient interaction between apoLF and CP. In contrast to LF, the interaction of apo-TF with CP is probably not stable within the physiological range of concentrations of TF.
AB - The year 2016 marked the 50th anniversary of the discovery by S. Osaki who first showed that ceruloplasmin (CP, ferro:O2-oxidoreductase or ferroxidase) is capable of oxidizing Fe(II) to Fe(III) and favors the incorporation of the latter into transferrin (TF). However, much debate remains in the literature concerning the existence of a complex between the enzyme oxidizing iron and the protein facilitating its transport in plasma. We studied CP in exocrine fluids and demonstrated its high-affinity interaction with transferrin found in breast milk and in lacrimal fluid, i.e. with lactoferrin (LF). Here we present data obtained by comparing the interaction of CP with LF and TF using surface plasmon resonance and Hummel–Dreyer chromatography. Binding of apo-LF within the range of concentrations 1.6-51.3 μM with CP immobilized on a CM5-chip is characterized by KD = 1.07 μM. Under similar conditions, the KD for apo-TF was measured and appeared to be higher than 51.3 μM. Hummel–Dreyer chromatography of CP with 51 μM apo-LF/apo-TF in the effluent demonstrated the absence of interaction between apo-TF and CP in solution, contrary to efficient interaction between apoLF and CP. In contrast to LF, the interaction of apo-TF with CP is probably not stable within the physiological range of concentrations of TF.
KW - ceruloplasmin
KW - Hummel–Dreyer chromatography
KW - lactoferrin
KW - protein–protein interaction
KW - surface plasmon resonance
KW - transferrin
UR - http://www.scopus.com/inward/record.url?scp=85029542634&partnerID=8YFLogxK
U2 - 10.1134/S0006297917090115
DO - 10.1134/S0006297917090115
M3 - Article
C2 - 28988537
AN - SCOPUS:85029542634
VL - 82
SP - 1073
EP - 1078
JO - Biochemistry (Moscow)
JF - Biochemistry (Moscow)
SN - 0006-2979
IS - 9
ER -
ID: 42247786