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Department of Dairy Husbandry, University of Illinois
Department of Chemistry, University of Illinois
ABSTRACT
By x-ray diffraction analysis an attempt has been made to interpret changes that were produced by the action of acids, alkalis and formaldehyde on casein, as well as, attempting to distinguish differences in casein prepared by various methods.
No marked differences were found in the casein samples prepared by various procedures. Only by vigorous boiling in the presence of NaOH were marked changes in structure observed due to chemical treatment.
The two halos produced by casein upon x-ray diffraction analysis were typical of non-fibrous proteins. The halos were at spacings of approximately 4.6 Å and 9.8 Å which correspond respectively to the vertical distance between layers of polypeptide chains and the longitudinal distance of side chains from the main chain. These values agree well with other non-fibrous proteins that have been subjected to x-ray analysis.
* The data presented in this paper are from a thesis submitted to the Graduate School of the University of Illinois in partial fulfillment of the degree of Doctor of Philosophy, 1937.
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