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J. Gross (1958)
Influence of Time on the Reversible Association between Large Molecules: the Collagen SystemNature, 181
(1958)
Neutral salt extractible components of skin of scorbutic guinea pigs
(1958)
The effect of various parameters on the rate of formation of fibers from collagen solutions
D. Jackson, J. Fessler (1955)
Isolation and Properties of a Collagen soluble in Salt Solution at Neutral pHNature, 176
J. Ferry (1948)
Protein gels.Advances in protein chemistry, 4
J. Gross (1956)
THE BEHAVIOR OF COLLAGEN UNITS AS A MODEL IN MORPHOGENESISThe Journal of Biophysical and Biochemical Cytology, 2
Combinaisons in vitro collag~ne-mucopolysac-FORMATION O~F COLLAGEN
(1957)
Heat reversible coagulation of some water soluble amino acid copolymers
J. Gross, J. Highberger, Francis Schmitt (1955)
EXTRACTION OF COLLAGEN FROM CONNECTIVE TISSUE BY NEUTRAL SALT SOLUTIONS.Proceedings of the National Academy of Sciences of the United States of America, 41 1
M. Lauffer, A. Ansevin, T. Cartwright, C. Brinton (1958)
Polymerization-depolymerization of tobacco mosaic virus protein.Nature, 181 4619
(1957)
Fractionation of neutral salt soluble collagen having temperature dependence of solubility
(1951)
Cross linkage in protein chemistry
David Jackson (1957)
Connective tissue growth stimulated by carrageenin. I. The formation and removal of collagen.The Biochemical journal, 65 2
W. Banfield (1952)
The solubility and swelling of collagen in dilute acid with age variations in manThe Anatomical Record, 114
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The metabolism of collagen and other proteins of the skin of rabbits.The Biochemical journal, 56 4
(1956)
charides et modifications apporte6s ~. ces combinaisons par des sels et des polyosides bacteriens, Connedi~e Tissue. A Symposium
(1956)
Some aspects of the stability and reactivity of collagens
(1952)
Procollagens, their chemical structure and biological function
J. Gross, D. Kirk (1958)
The heat precipitation of collagen from neutral salt solutions: some rate-regulating factors.The Journal of biological chemistry, 233 2
Precipitation (or gelation) of collagen from cold neutral salt solution induced by warming was shown to be reversible on subsequent cooling. The degree of reversibility of heat precipitation rapidly diminished with time of incubation at 37°C. For calf skin collagen (acetic acid-extracted) and guinea pig skin collagen (crude NaCl extract) in neutral salt solutions (Γ/2 = 0.45) roughly 90 per cent of newly formed gel redissolved on cooling at 2°C.; less than 20 per cent redissolved on cooling gels previously maintained at 37°C. for 24 hours. At physiologic ionic strength the same preparations exhibited much more rapid development of irreversible precipitation, but the same time dependence was clearly evident. Highly purified collagen from crude saline extracts of guinea pig skin exhibited the same phenomenon although the quantitative aspects were somewhat different. Footnotes Submitted: 26 March 1958
The Journal of Experimental Medicine – Rockefeller University Press
Published: Aug 1, 1958
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