Magnetization transfer in cross-linked bovine serum albumin solutions at 200 MHz: a model for tissue.

Abstract

We report results for proton 1/T1, 1/T2, and K, the rate of magnetization transfer from solvent to solute, for 5 and 10 wt. % solutions of bovine serum albumin, both native and chemically cross-linked, in undeuterated and approximately 50% deuterated water, at 4.7 T (200.1 MHz) and 19 degrees C. At this field, although K > 1/T1 for the cross-linked samples, magnetization transfer contributes little to 1/T1 directly. Therefore K was measured using off-resonance irradiation of the protein protons. The data for all the samples can be fit using a theoretical model for magnetization transfer, with three parameters: the intrinsic longitudinal relaxation rates of solute and solvent protons, and K. The magnitude of K is so large that the newly-identified, long-lived (approximately 1 microseconds) hydration sites (S.H. Koenig, R.D. Brown III, and R. Ugolini, Magn. Reson. Med., 29, 77 (1993)) must be invoked to account for K, as is necessary to explain the differential effects of cross linking on the magnetic field dependence of 1/T1 of protons and deuterons and the large 1/T1 and 1/T2 values below approximately 20 MHz in immobilized systems. Although these sites are few in number, their long resident lifetime becomes the correlation time for magnetization transfer when protein is immobilized, accounting for the large value of K. Recent data from several laboratories have shown that cross-linked protein, as used here, is a good model for 1/T1 and 1/T2 of tissue, as a function of temperature and magnetic field.