MAGNETIZATION TRANSFER IN CROSS-LINKED BOVINE SERUM-ALBUMIN SOLUTIONS AT 200 MHZ - A MODEL FOR TISSUE
MAGNETIZATION TRANSFER IN CROSS-LINKED BOVINE SERUM-ALBUMIN SOLUTIONS AT 200 MHZ - A MODEL FOR TISSUE
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DOI:
10.1002/mrm.1910290306
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发表时间:
1993-03-01
影响因子:
3.3
通讯作者:
UGOLINI, R
中科院分区:
文献类型:
--
作者:
KOENIG, SH;BROWN, RD;UGOLINI, R
We report results for proton 1/T1, 1/T2, andK, 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 ∼50% deuterated water, at 4.7 T (200.1 MHz) and 19°C. At this field, althoughK> 1/T1for the cross‐linked samples, magnetization transfer contributes little to 1/T1directly. ThereforeKwas 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, andK. The magnitude ofKis so large that the newly‐identified, long‐lived (∼1 μs) hydration sites (S. H. Koenig, R. D. Brown III, and R. Ugolini, Magn. Reson. Med., 29, 77 (1993)) must be invoked to account forK, as is necessary to explain the differential effects of cross linking on the magnetic field dependence of 1/T1of protons and deuterons and the large 1/T1and 1/T2values below ∼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 ofK. Recent data from several laboratories have shown that cross‐linked protein, as used here, is a good model for 1/T1and 1/T2of tissue, as a function of temperature and magnetic field.