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Oriented Crystallization of Urea in Membranes

Published online by Cambridge University Press:  06 March 2019

Edwin H. Shaw Jr.
Edwin H. Shaw Jr.*
Affiliation:
University of South Dakota, Vermillion, South Dakota
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Abstract

Inner egg shell membrane was soaked in 2 M urea solution and dried. Cu Kα X-rays directed perpendular to the membrane yielded an urtsymmetrical diffraction pattern with urea 110, 111, 102, 210 and 211 planes diffracting to the right and urea 101, 200 and 201 planes diffracting to the left. The urea appears to be hydrogenbonded diagonally between the lamellae of β-keratin at an angle of 33.5° to the 6.68 Å b-axis (fiber axis) of the parallel pleated sheet structure, shortening the half-axis lengths in the a direction from 4.73 Å to 4.41 Å. Similar results were obtained with formalinized dog mesentery. Keratinous outer egg shell membrane, formal in bed collagenous dog renal capsule, formslinized collagenous pheasant pericardium, and formalinized callogenous human arachnoid yielded symmetrically oriented urea layer lines. Formalinized dog renal fascia and pleura yielded random urea lines.

Type
Research Article
Information
Advances in X-Ray Analysis , Volume 9: Fourteenth Annual Conference on Applications of X-ray Analysis, August 25-27, 1965 , 1965 , pp. 190 - 193
Copyright
Copyright © International Centre for Diffraction Data 1965

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References

1. Shaw, E. H. Jr., “Oriented Crystallization of Amides on Collagen with Modification of the Collagen Lattice,” in: W. M. Mueller, G. R. Mallett, and M. J. Fay (eds.), Advances in X-ray Analyst, Vol. 7, Plenum Press, New York, 1964, p. 252.Google Scholar
2. Shaw, E. H., J. and Christensen, Alton R., “Modification of Collagen and Nylon Lattices by Resorcinoi,” in: W. M. Mueller, G. R. Mallett, and M. J. Fay (eds.), Advances in X-Ray Analysis, Vol. 8, Plenum Press, New York, 1965, p. 175.Google Scholar
3. Gilkerson, W. R. and Srivastava, K. K., “The Dipole Moment of Urea,” J. Phys. Chem, 64: 1485, 1960.Google Scholar
4. Calvery, H. O., “Some Analyses of Egg Shell Keratin,” J. Biol. Ckem. 100: 183, 1933.Google Scholar
5. Moran, T. and Hale, H. P., “Physics of the Hen's Egg. I. Membranes in the Egg,” J. Exptl. Biol. 13: 35, 1936.Google Scholar
6. Fraser, R. D. B. and MacRae, T. P., “An Investigation of the Structure of β-Keratin,” J. Mol. Biol. 5: 457, 1962.Google Scholar