Abstract
X-ray diffraction studies were conducted on calcified turkey leg tendon to establish the effect of mineralization on some of the structural properties of collagen. The principal finding was that the first equatorial reflection of collagen in freshly-excised calcified tendon had a d-spacing intermediate between the values for dried collagen and fresh unmineralized collagen. Since this spacing is a sensitive monitor of moisture levels in collagen, the data suggest that mineralization reduces the amount of water than can associatein vivo with the collagen component in tissue. It was also found that the presence of mineral appears to increase the resistance of collagen to permanent thermal denaturation.
Résumé
Des études de diffraction aux rayons X sont réalisées au niveau du tendon calcifié de la patte de dinde pour déterminer l'effet de la minéralisation sur certaines propriétés structurales du collagène. Le résultat le plus important indique que la première raie équatoriale du collagène de tendon calcifié, fraichement prélevé, présente une équidistance intermédiaire entre les valeurs de collagène déssèché et du collagène frais non calcifié. Comme cette équidistance parait traduire fidèlement le degré d'humidité du collagène, il semble que la minéralisation réduit la quantité d'eau associéein vivo avec le composant collagènique du tissu. La présence du minéral semble augmenter la résistance du collagène à une dénaturation thermique permanente.
Zusammenfassung
Es wurden Röntendiffraktionsuntersuchungen an calcifizierten Truthahnbeinsehnen durch geführt, um die Wirkung der Mineralisation auf einige der strukturellen Eigenschaften von Collagen festzustellen. Die wichtigste Beobachtung war, daß die erste äquatoriale Reflexion von Collagen in frish herauspräparierten calcifizierten Sehnen einen d-Wert aufwies, der zwischen den Werten für trockenes Collagen und frisches, nicht mineralisiertes Collagen liegt. Da dieser d-Wert empfindlich auf den Feuchtigkeitsgrad des Collagens reagiert, lassen diese Resultate vermuten, daß die Mineralisation die Wassermenge reduziert, welche sich in vivo mit der Collagenkomponente im Gewebe verbinden kann. Es wurde auch beobachtet, daß die Anwesenheit von Mineral den Widerstand von Collagen gegen bleibende thermale Denaturierung heraufzusetzen scheint.
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References
Bear, R. S.: X-ray diffraction studies on protein fibers I. The large fiber-axis period of collagen. J. Amer. chem. Soc.66, 1297–1305 (1944).
—: The structure of collagen fibrils. Advanc. in Protein Chem.7, 69–160 (1952).
Chesley, F. G.: X-ray diffraction camera for microtechniques. Rev. Sci. Instrum.18, 422–424 (1947).
Deakins, M.: Changes in the ash, water, and organic content of pig enamel during calcification. J. dent. Res.21, 429–435 (1942).
Eanes, E. D., Miller, E. J.: Effect of covalent cross-linking on the x-ray diffraction properties of chick bone and rat tail tendon collagens. Arch. Biochem.129, 769–771 (1969).
Engstrom, A.: Apatite-collagen organization in calcified tendon. Exp. Cell Res.43, 241–245 (1966).
Haker, A., Runyon, R. P.: General statistics, p. 188. Reading, Mass: Addison-Wesley 1969.
Hodge, A. J.: Structure at the electron microscopic level. In: Treatise on collagen, vol. I (G. N. Ramachandran, ed.), p. 185–205. New York and London: Academic Press 1967.
—, Petruska, J. A.: Recent studies with the electron microscope on ordered aggregates of the tropocollagen molecule. In: Aspects of protein structure (G. N. Ramachandran, ed.), p. 289–300. London and New York: Academic Press 1963.
Miller, E. J., Martin, G. R., Piez, K. A., Powers, M. J.: Characterization of chick bone collagen and compositional changes associated with maturation. J. biol. Chem.242, 5481–5489 (1967).
Myers, H. M., Engstrom, A.: A note on the organization of hydroxyapatite in calcified tendons. Exp. Cell Res.40, 182–185 (1965).
Nylen, M. U., Scott, D. B., Mosley, V. M.: Mineralization of turkey leg tendon. II. Collagen-Mineral relations revealed by electron and x-ray microscopy. In: Calcification in biological systems (R. F. Sognnaes, ed.), p. 129–142. Americal Association for the Advancement of Science, Washington, D. C., 1960.
Piez, K. A., Eigner, E. A., Lewis, M. S.: The chromatographic separation and amino acid composition of the subunits of several collagens. Biochemistry2, 58–66 (1963).
Ramachandran, G. N.: Structure of collagen at the molecular level. In: Treatise on collagen, vol. I (G. N. Ramachandran, ed.), p. 103–183. New York and London: Academic Press 1967.
Robinson, R. A.: Chemical analysis and electron microscopy of bone. In: Bone as a tissue (K. Rodahl, J. T. Nicholson, and E. M. Brown, eds.), p. 186–250. New York: McGraw-Hill 1960.
Rougvie, M. A., Bear, R. S.: An x-ray diffraction investigation of swelling by collagen. J. Amer. Leather Chemists Assoc.48, 735–751 (1953).
Scott, D. B., Nylen, M. U., Pugh, M. H.: Some technical aspects of microradiography. Norelco Reporter9, 103–109 (1962).
Witnauer, L. P.: The relationship between shrinkage of hide and the crystal-liquid transition of collagen. In: Collagen (N. Ramanathan, ed.), p. 441–451. New York: Interscience 1962.
Wright, B. A., Wiederhorn, N. M.: Studies concerned with the structure of collagen. I. An. x-ray investigation of the denaturation of collagen. J. Polymer Sci.7, 105–120 (1951).
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Eanes, E.D., Lundy, D.R. & Martin, G.N. X-ray diffraction study of the mineralization of turkey leg tendon. Calc. Tis Res. 6, 239–248 (1970). https://doi.org/10.1007/BF02196204
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DOI: https://doi.org/10.1007/BF02196204