In a preceding paper were reported the results of an x-ray investigation of the dimensions and configurations of certain nerve lipides both in the wet and dry condition (Bear, Palmer arid Schmitt, '41). Particularly striking was the fact that, in the case of lipide mixtures, although the individual
X-ray diffraction studies of nerve lipides
โ Scribed by Bear, Richard S. ;Palmer, Kenneth J. ;Schmitt, Francis O.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1941
- Tongue
- English
- Weight
- 692 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0095-9898
No coin nor oath required. For personal study only.
โฆ Synopsis
Since lipide molecules enter prominently into the structure of many protoplasmic constituents (for reviews see Schmidt, '37 ; Schmitt, '39) it is desirable to understand the way in which these molecules pack in oriented layers, their approximate dimensions and configurations, and the effect of the chemical environment upon these properties. The present investigation, devised to answer some of these questions, arose from previous studies of the molecular structure of the nerve myeliii sheath (Schmitt, Bear and Clark, '35; Schmitt and Bear, '39) which demonstrated the presence in this structure of an identity period of approximately 170 A. It was assumed that this period was produced by a mixed-component system consisting of lipide and protein. A more detailed interpretation was impossible, however, until data were available concerning the diffraction patterns of the pure lipides both in single arid in mixed systems. The subject is of interest also to the lipide chemist since the x-ray analysis provides another means of determining the characteristics of individual components, as well as to those interested in coacervation phenomena involving lipides (see, for example, Bungenberg de Jong and Saubert, '37).
Methods
Our immediate interest lay in the interpretation of nerve diffraction patterns, hence the lipides were extracted exclusively from nervous tissue. Lecithin, cephalin, sphingomyelin, kerasin and phrenosin were isolated from beef spinal cord by methods outlined by Thierfelder and Klenk ('30
๐ SIMILAR VOLUMES
Cephalin readily combines with basic proteins, such as histones, forming a precipitate which may be insoluble in water and organic solvents (Chargaff, '38; Chargaff and Ziff, '39). From the combining ratios it was shown that cephalin, which is acidic, combines with basic proteins through salt linkag