Comparative intermolecular cross-relaxation studies of human hemoglobin in red blood cells and bovine serum albumin in solution.

Intermolecular cross-relaxation rate (CR) spectra [1/T(IS) (HDO) or 1/T(IS) (H(2) O) vs f(2) (ppm) profiles] for bovine serum albumin [BSA; molecular weight (MW), 66 kDa] solution, partially hydrolyzed BSA gel (BSA*gel) and packed human red blood cells (RBCs) with normal or unstable hemoglobin (Hb; MW, 65 kDa) were studied using f(2) irradiation ranging from - 100 to 100 ppm at γH(2) /2π of 250 Hz. The CR spectra for BSA*gel (pD 4.01, 0.

Comparative 1H NMR studies of saturation transfer in copolymer gels and mouse lenses.

Saturation transfer in cross-linked copolymer gels and excised intact and perforating trauma-induced cataract mouse lenses (4- or 8-week-old) were studied using intermolecular cross-relaxation rates (1/T(IS)(H(2)O); 1/T(IS)), monitored with f(2)-irradiation at -8.79, -4.00, and 7.

Comparative 1H NMR studies on the structural looseness of the aged (A) and non-aged (N) bovine mercaptalbumin in the alkaline region.

Bovine serum albumin (BSA) and mercaptalbumin (BMA) exhibit the N-B transition in the alkaline region (pH 7.0-->9.0).