scholarly journals The denaturation of acetic acid-soluble calf-skin collagen. Changes in optical rotation, viscosity and susceptibility towards enzymes during serial denaturation in solutions of urea

1962 ◽  
Vol 85 (1) ◽  
pp. 207-210 ◽  
Author(s):  
FS STEVEN ◽  
GR TRISTRAM
Keyword(s):  
Acetic Acid ◽  
Optical Rotation ◽  
Skin Collagen ◽  
Calf Skin

scholarly journals The effect of ultraviolet irradiation on soluble collagen

1965 ◽  
Vol 97 (1) ◽  
pp. 139-147 ◽  
Author(s):  
DR Cooper ◽  
RJ Davidson
Keyword(s):  
Ultraviolet Irradiation ◽  
Optical Rotation ◽  
Gel Filtration ◽  
Collagen Molecule ◽  
Neutral Salt ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Skin Collagen ◽  
Kinetics Of ◽  
Calf Skin

1. The effect of ultraviolet irradiation on acid-soluble and neutral-salt-soluble calf-skin collagen was studied by chromatography, gel filtration, amino acid analysis and sedimentation of the sub-units, and the reaction kinetics of degradation were obtained from viscosity and optical rotation measurements. 2. It was demonstrated that, whereas the structure of neutral-salt-soluble calf-skin collagen may be represented by the formula (alpha(1))(2)alpha(2), the acid-soluble extract has the formula alpha(1).(alpha(2))(2). The acid-soluble collagen is also unusual in containing a large amount of a component that could be beta(22). 3. Ultraviolet irradiation causes the progressive degradation of the collagen molecule into smaller molecular fragments that subsequently lose their helical nature. The rate constants show that the denaturation of soluble collagens by ultraviolet irradiation is much slower, under the conditions used, than denaturation by heat or enzymes.

scholarly journals The effect of glycols on the renaturation of soluble collagen

1971 ◽  
Vol 125 (4) ◽  
pp. 1069-1074 ◽  
Author(s):  
D. R. Cooper ◽  
A. E. Russell ◽  
G. J. Hart
Keyword(s):  
Optical Rotation ◽  
Fixed Time ◽  
Native Protein ◽  
Fixed Temperature ◽  
Recovery Rates ◽  
Skin Collagen ◽  
Initial Recovery ◽  
The Relationship ◽  
Kinetics Of ◽  
Calf Skin

The effects of a number of related glycols and substituted glycols on the renaturation kinetics of acid-soluble calf-skin collagen have been investigated. Optical rotation recovery was monitored at a fixed temperature in the presence of perturbants and the initial rates of reaction were determined. The effects of perturbants on stability of the native protein are compared with their action in the renaturing systems. The relationship between initial recovery rates and fixed-time [α]-values is shown to be dependent upon the renaturation temperature. The influence of perturbant concentration on recovery rates is discussed in terms of present theories of the mechanism of collagen renaturation.

scholarly journals STUDIES ON THE FORMATION OF COLLAGEN

1958 ◽  
Vol 108 (2) ◽  
pp. 215-226 ◽  
Author(s):  
Jerome Gross
Keyword(s):  
Acetic Acid ◽  
Ionic Strength ◽  
Guinea Pig ◽  
Salt Solution ◽  
Rapid Development ◽  
Neutral Salt ◽  
Salt Solutions ◽  
Pig Skin ◽  
Skin Collagen ◽  
Calf Skin

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.

scholarly journals The origin of N-terminal residues in acetic acid-soluble calf-skin collagen

1962 ◽  
Vol 83 (2) ◽  
pp. 245-248 ◽  
Author(s):  
FS STEVEN ◽  
GR TRISTRAM
Keyword(s):  
Acetic Acid ◽  
Skin Collagen ◽  
Calf Skin

scholarly journals The Location of Cross-links in γ Chains from Calf Skin Collagen

1968 ◽  
Vol 243 (11) ◽  
pp. 2890-2898
Author(s):  
M P Drake ◽  
P F Davison
Keyword(s):  
Skin Collagen ◽  
Cross Links ◽  
Calf Skin

scholarly journals The Viscometric Behavior of Solubilized Calf Skin Collagen at Low Rates of Shear

1966 ◽  
Vol 241 (8) ◽  
pp. 1784-1789
Author(s):  
Leo D. Kahn ◽  
Lee P. Witnauer
Keyword(s):  
Skin Collagen ◽  
Calf Skin
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