Noninvasive measurement of protein concentration

✍ Scribed by Xiaoqi Jiao; Robert G. Bryant

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 277 KB
• Volume: 35
• Category: Article
• ISSN: 0740-3194
• DOI: 10.1002/mrm.1910350205

✦ Synopsis

Abstract

At selected magnetic field strengths, protein and water proton spin‐lattice relaxation rates are sensitive to the concentration of rotationally immobilized peptide nitrogen because of field dependent heteronuclear cross relaxation coupling between protein proton and nitrogen‐14 spins that is carried to the water by proton homonuclear cross‐relaxation. Measurement of the water proton spin‐lattice relaxation time, or a signal amplitude proportional to it, may provide a noninvasive measure of peptide bond concentration, which provides a direct measure of immobilized protein content in most tissues. The approach using protein gels in two magnetic field strengths is demonstrated. At 66.7 mT, the proton Zeeman energy matches one of the peptide nitrogen transitions dominated by the unaveraged nuclear electric quadrupole interaction; cross‐relaxation between the protons and nitrogen‐14 is efficient At 77.5 mT, the proton Zeeman energy is not matched with the nitrogen energy and proton‐nitrogen cross‐relaxation is not efficient. It is shown that the difference in the water proton spin‐lattice relaxation rates on and off the energy level match condition is a linear function of the rotation‐ally immobilized protein concentration.