Nuclear relaxation in serum protein mixtures and serum samples.
The Nuclear Magnetic Relaxation Dispersion (NMRD) profiles of water protons in aqueous solutions containing various total amounts of human serum protein (5-14 pcw) in identical macro molecular ratios (60% of albumin, 20% of gamma globulins, and 20% of other globulins) were studied to examine the influence of the individual relaxation properties of the proteins on the global relaxation time of their mixture. The "synthetic" profiles calculated from the single protein relaxivities overlap with the experimental NMRD data for protein mixtures; similar results were obtained for the relaxation rates measured at 27 MHz of the serum samples from patients with different cancer diseases. The results confirm that the global relaxation of serum is determined by the relaxation of the basic serum proteins.
Department of Physics, Agricultural University, Poznan, Poland.
K J
KJ
Olszewski
H M
HM
Baranowska
D001798:Blood Proteins / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D009369:Neoplasms / Q000097:blood; D011522:Protons; D014867:Water / Q000737:chemistry
D001798:Blood Proteins; D011522:Protons; D014867:Water