The Murayama Test. Part I. Evidence for the Modified Murayama Hypothesis for the Molecular Mechanism of Sickling.
Abstract
An analytical review of the literature yields considerable support for the recently modified Murayama hypothesis for the molecular mechanism of sickling in S hemoglobin. The Murayama concept implicates as essential to the sickling event in S hemoglobin specified hydrophobic bonds between interacting tetramers. Hydrophobic bonds have recently been recognized to be predominantly responsible for the steric configuration of proteins in aqueous systems. Furthermore, it is shown that the helical stability of proteins in aqueous systems is the result of counter-poised actions of hydrogen and hydrophobic bond strengths as a function of temperature. Application of this basic, general concept is made in the special case of the Murayama Test. Also, the molecular configuration of the S hemoglobin tetramer and its critical relationship to the formation of hydrophobic bonds between interacting tetramers is noted. The Murayama Test is shown to discriminate specifically for S hemoglobin on the basis of molecular structure and is presented as the first test for the detection of the specific molecular lesion of S hemoglobin. The details of the principle, technique, and experimental data of the Murayama Test are reported in Part II. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 17, 1970
- Accession Number
- AD0715248
Entities
People
- Bruce M. Nichols
- Frank R. Camp Jr.
- Paul L. Wolf
- Raymond L. Henry
- Robert M. Nalbandian
Organizations
- United States Army Medical Research Laboratory