[The effect of nucleotides on oligomeric state of human lactoferrin].
A polyfunctional protein lactoferrin (LF) which is present in human barrier fluids, blood and milk and this protein of acute phase is responsible for nonspecific cells defense against microbial and viral infection and cancer diseases. Using the methods of small-angle X-ray scattering and light-scattering it was shown that LF in solution exists in oligomeric state. The level of LF oligomerization depends upon its concentration and time of keeping of no frozen neutral protein solutions. At the concentrations comparable with those in human milk (1-6 mg/ml) the average inertial radius values (Rg) of LF can reach 100-450 angstroms, while Rg for monomer LF form is 26.7 angstroms. LF was shown to complex with different nucleotides and hydrolyze them. The addition of ATP and AMP to LF demonstrating any level of oligomerization leads to increase of oligomerization processes and enhancement of the Rg values up to 600-700 angstroms According to different models of LF monomer association to its oligomeric forms (sphere, plate, cylinder) the oligomeric complexes demonstrate high Rg values which can contain from several tens up to several thousands of LF monomers. A possible role of LF oligomerization for different biological functions of the protein is discussed.
Babina
S E
SE
Tuzikov
F V
FV
Tuzikova
N A
NA
Buneva
V N
VN
Nevinskiĭ
G A
GA
D000249:Adenosine Monophosphate / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000737:chemistry; D019281:Dimerization; D005260:Female; D006801:Humans; D007781:Lactoferrin / Q000737:chemistry*; D008027:Light; D008895:Milk, Human / Q000737:chemistry*; D008956:Models, Chemical; D012542:Scattering, Radiation; D014961:X-Ray Diffraction; D014965:X-Rays
D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D007781:Lactoferrin