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Collagen chemistry

Much of the knowledge of soluble collagen chemistry derives from initial papers by Tustanovskii (1947) and Orekhovich d al. (1948a,b) who demonstrated a reversible solubility of collagen fibrils that had dissolved in citric acid buffers (pH 3-4.5) and underwent reformation into collagen fibrils upon dialysis against water. [Pg.308]

T. C. Thorstensen, Fundamentals of Pollution Controlfor the Eeather Industy, Shoe Trades Publishing Co., Cambridge, Mass., 1993 K. H. Gustavson, The Chemistry and Keactivity of Collagen, Academic Press, Inc., New York, 1956. [Pg.87]

K. H. Gustavson, The Chemistry and Reactivity of Collagen, Academic Press, New York (1956). [Pg.437]

Tykot, R.H., van der Merwe, N.J. and Hammond, N. 1996 Stable isotope analysis of bone collagen, bone apatite, and tooth enamel in the reconstruction of human diet. A case study from Cuello, Belize. In Orna, M.V., ed., Archaeological Chemistry Organic, Inorganic, and Biochemical Analysis. ACS Symposium Series 625, Washington, DC, American Chemical Society 355-365. [Pg.37]

Harrington, W.F. von Hippel P.H. The stricture of collagen and gelatin. Advances in Protein Chemistry, 16 (1962) 1-138. [Pg.113]

Structure, chemistry and preservation potential of bone collagen... [Pg.142]

Mithieux SM, Weiss AS (2005) Elastin. In Parry DAD, Squire JM (eds) Fibrous proteins coiied-coiis, collagen and elastomers. Advances in protein chemistry, vol 70. Elsevier Academic, San Diego, pp 437-461... [Pg.110]

Ackerman, M.S., Bhate, M., Shenoy, N., Beck, K., Ramshaw, JA.M. and Brodsky, B. (1999) Sequence dependence of the folding of collagen-like peptides - single amino acids affect the rate of triple-helix nucleation. Journal of Biobgical Chemistry 274, 7668-7673. [Pg.194]

Bachinger, H.P. (1987) The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagens. Journal of Biobgical Chemistry 262, 17144-17148. [Pg.194]

Engel, J. and Prockop, D.J. (1991) The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper. Annual Review of Biophysics and Biophysical Chemistry 20, 137—152. [Pg.195]

Lamberg, A., Helaakoski, T., Myllyharju, J., Peltonen, S., Notbohm, H., Pihlajaniemi, T. and Kivirikko, K.I. (1996) Characterization of human type III collagen expressed in a baculovirus system - production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit.Journal of Biological Chemistry 271, 11988-11995. [Pg.197]

Steinmann, B., Bruckner, P. and Superti-Furga, A. (1991) Cyclosporin A slows collagen triple-helix formation in vivo indirect evidence for a physiological role of peptidyl prolyl cis-trans isomer use. Journal ofBiological Chemistry 266,1299-1303. [Pg.200]

Aryal, S., Bahadour, K.C.R., Bhattarai, J.R., Prabu, P. and Kim, H.Y. (2006) Immobilization of collagen on gold nanoparticles, preparation, characterization and hydroxyapatite growth, foumal of Materials Chemistry, 16, 4642-4648. [Pg.189]

Hassan, A. A., Hare, P. E., Amino Acid Analysis in Radiocarbon Dating of Bone Collagen, In Archaeological Chemistry II, p. 109-116, Washington, D.C., American Chemical Society, 1978. [Pg.466]

D. Greenspan, Biosynthetic Processing of Collagen Molecules. In Collagen Primer In Structure, Processing and Assembly Topics in Current Chemistry, J. Brinckmann, H. Notbohm, P. K. Muller, Eds. Springer Berlin Heidelberg New York, 2005 pp 149-183. [Pg.526]


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See also in sourсe #XX -- [ Pg.28 , Pg.240 , Pg.241 , Pg.242 , Pg.243 , Pg.244 , Pg.245 , Pg.246 , Pg.247 , Pg.248 , Pg.249 ]




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Collagen soluble chemistry

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