Abstract
The Murayama test, a new, specific test for S hemoglobin, is based on the molecular mechanism of sickling for S hemoglobin proposed by Murayama [Clin. Chem. 14, 578 (1967)]. The test depends on a feature of molecular structure: hydrophobic bonds formed between interacting tetramers by the no. 6 valine, which is substituted for glutamic acid near the N-terminal end of each β S globin chain. Existence of these particular hydrophobic bonds is manifested in deoxygenated, concentrated hemolysates by reversible sol— gel transformations at 0° and 37°C. In such systems, demonstration of reversible, temperature-dependent sol—gel transformations (a negative temperature coefficient of gelation) is specific for S hemoglobin or the S structural variant, hemoglobin C (Harlem). The test is simple, has clear endpoints, will detect both homozygous and heterozygous S hemoglobin, and is specific. A practical approach is suggested to the precise identification of S and non-S sickling hemoglobins in the diagnostic laboratory. The close agreement between Murayama’s hypothesis for sickling in S hemoglobin and our results with 29 cases of S hemoglobin and 37 controls further support his views.
Selectivity of Tungsten Oxide Synthesized by Sol-Gel Method Towards Some Volatile Organic Compounds and Gaseous Materials in a Broad Range of Temperatures