Koenig S H, Brown R D, Adams D, Emerson D, Harrison C G
Invest Radiol. 1984 Mar-Apr;19(2):76-81. doi: 10.1097/00004424-198403000-00002.
It is well established that the spin-lattice magnetic relaxation rate 1/T1 of solvent protons in homogeneous protein solutions increases dramatically as the magnetic field is reduced well below the traditional NMR range. For a 5% solution of protein of 10(5) Daltons, for example, 1/T1 increases from about 50% above the pure solvent rate at 20 MHz to five times the solvent rate at 0.01 MHz. At higher fields, the effect of protein on the relaxation rate decreases progressively toward zero. 1/T1 of solvent in erythrocyte suspension behaves similarly, indicating that extracellular water has ready access to intracellular protein. We now report analogous data for samples of various mammalian tissues: we find that the data can be accommodated within the conceptual framework developed earlier for analyzing homogeneous protein solutions. It appears that tissue water probes the macromolecular composition and structure in a tissue-specific fashion. The variation of 1/T1 with field differs for each tissue, and its magnitude at low fields varies by more than a factor of three, far more than does the water content of the tissues. The relevance to contrast in NMR imaging is discussed.
众所周知,在均匀蛋白质溶液中,当磁场降低到远低于传统核磁共振范围时,溶剂质子的自旋 - 晶格磁弛豫率1/T1会急剧增加。例如,对于一种分子量为10⁵道尔顿的蛋白质的5%溶液,1/T1从20兆赫兹时比纯溶剂速率高约50%增加到0.01兆赫兹时是溶剂速率的五倍。在更高磁场下,蛋白质对弛豫率的影响逐渐减小至零。红细胞悬液中溶剂的1/T1表现类似,表明细胞外水可以很容易地接触到细胞内蛋白质。我们现在报告各种哺乳动物组织样本的类似数据:我们发现这些数据可以纳入先前为分析均匀蛋白质溶液而建立的概念框架内。似乎组织水以组织特异性方式探测大分子组成和结构。每个组织的1/T1随磁场的变化不同,其在低磁场下的大小变化超过三倍,远超过组织中的水含量变化。讨论了其与核磁共振成像中对比度的相关性。