Ultratrace Lithium and Boron Analysis by Neutron Activation and Helium Isotope Mass Spectrometry

Abstract

The binding of the elements lithium and boron to human plasma proteins is investigated through the techniques of thermal neutron activation and helium isotope mass spectrometry. Since normal physiological levels of lithium and boron in blood and plasma are in the ultratrace (ppb) range, lithium in particular is frequently below the detection limit of many instruments. The success of the detection method used in this work is due to the extremely large cross section of ⁶Li for the thermal neutron reaction ⁶Li(n,³H)⁴He, and of ¹⁰B for the thermal neutron reaction ¹⁰B(n,α)⁷Li. The high sensitivity of the mass spectrometer, originally designed for oceanographic studies of helium isotopes and tritium, allows measurement of as little as 2x10⁴ atoms of ³He from the decay of tritium, and 2x10¹⁰ atoms of ⁴He from alpha-particles. It has frequently been stated that lithium does not bind to plasma proteins. However, our results clearly show that lithium does bind to a number of these proteins, at least 𝘪𝘯 𝘷𝘪𝘵𝘳𝘰. Boron is also shown to bind to proteins, with a pattern similar to that of lithium . Although a clear identification of the specific plasma proteins which bind lithium and boron must await further investigation, a number of possibilities are suggested here, based on the data obtained.