scholarly journals Some properties of neutral-salt-soluble collagen. 1

1960 ◽  
Vol 76 (3) ◽  
pp. 452-463 ◽  
Author(s):  
J. H. Fessler
Keyword(s):  
Neutral Salt ◽  
Soluble Collagen

scholarly journals Chemical changes associated with aging of collagen in vivo and in vitro

1969 ◽  
Vol 112 (4) ◽  
pp. 397-405 ◽  
Author(s):  
Kalindi Deshmukh ◽  
Marcel E. Nimni
Keyword(s):  
Absorption Spectrum ◽  
Neutral Salt ◽  
Unsaturated Aldehyde ◽  
Salt Solutions ◽  
Rat Skin ◽  
Soluble Collagen ◽  
Insoluble Collagen ◽  
Cross Links

Collagen extracted from rat skin by neutral-salt solutions contains less aldehydes than the more insoluble collagen fractions. The concentration of aldehydes in collagen is directly related to its capacity to form stable cross-linked gels, which do not redissolve on cooling and become more insoluble in a variety of reagents. Whereas the absorption spectrum of neutral-salt-soluble collagen treated with N-methylbenzothiazolone hydrazone resembles that of acetaldehyde, the more insoluble collagen fractions show increasing amounts of a component that behaves like an αβ-unsaturated aldehyde. The ratio between α- and β-sub-units present in a particular fraction of soluble collagen seems to be constant and independent of the age of the animal. Neutral-salt-soluble collagen, which has a low concentration of β-components, will generate intramolecular bonds if gelled at 37°. These intramolecular bonds seem to precede the formation of stable intermolecular cross-links, since these gels can redissolve when cooled to yield a soluble collagen with a higher content of β-components of intramolecular origin.

Intermolecular Relationship between Neutral-salt-soluble and Acid-soluble Collagen

Nature ◽  
1968 ◽  
Vol 217 (5124) ◽  
pp. 168-169 ◽  
Author(s):  
R. J. DAVIDSON ◽  
D. R. COOPER
Keyword(s):  
Neutral Salt ◽  
Soluble Collagen ◽  
Acid Soluble Collagen

scholarly journals The effect of ultraviolet irradiation on acid-soluble collagen

1967 ◽  
Vol 105 (3) ◽  
pp. 965-969 ◽  
Author(s):  
R. J. Davidson ◽  
D. R. Cooper
Keyword(s):  
Conformational Changes ◽  
Ultraviolet Irradiation ◽  
Irradiation Dose ◽  
Helical Structure ◽  
Neutral Salt ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Skin Collagen ◽  
Principal Effect ◽  
Chain Lengths

1. A study has been made of the effect of ultraviolet irradiation on the conformational changes taking place in cooled solutions of thermally denatured acid-soluble calf-skin collagen. 2. The increase in negative rotation and viscosity at 15° for irradiated and thermally denatured collagen solutions becomes less as the irradiation dose is increased. 3. The principal effect of ultraviolet irradiation is the fission of the primary collagen chains, eventually yielding chain lengths incapable of stabilizing a helical structure. 4. The effects of ultraviolet irradiation on acid-soluble collagen may be closely correlated with similar effects on neutral salt-soluble collagen.

scholarly journals Studies on Neutral Salt Soluble Collagen from Whale Nose Cartilage

1969 ◽  
Vol 35 (10) ◽  
pp. 1006-1011 ◽  
Author(s):  
Minoru KUBOTA ◽  
Naoyuki UCHIDA ◽  
Shigeru KIMURA
Keyword(s):  
Neutral Salt ◽  
Soluble Collagen

scholarly journals ULTRASTRUCTURAL LOCALIZATION OF A SOLUBLE COLLAGEN ANTIGEN

1971 ◽  
Vol 19 (11) ◽  
pp. 663-669 ◽  
Author(s):  
LIVIA LUSTIG
Keyword(s):  
Chick Embryo ◽  
Light And Electron Microscopy ◽  
Ultrastructural Localization ◽  
Ultrastructural Level ◽  
Collagen Fibrils ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Neutral Salt ◽  
Antibody Technique ◽  
Soluble Collagen

Soluble collagen antigen was localized at the ultrastructural level using an enzyme-labeled antibody technique. Specific antiserum against neutral salt-soluble collagen was conjugated with horseradish peroxidase. Tissue culture of fibroblasts, sections of chick embryo connective tissue and skin and tendon of newborn and adult chickens were incubated with the conjugated antiserum and processed for light and electron microscopy. Light microscopic observations showed a localization of the collagen antigen in the cytoplasm of fibroblasts and in the extracellular collagen fibers. Ultrastructurally, the antigen was found on the ribosomes, on the membranes of the rough endoplasmic reticulum, in the intracisternal material of fibroblasts and extracellularly in the collagen fibrils. The collagen fibrils of chick embryo cartilage were intensely stained while the matrix itself remained unstained. Controls performed with absorbed antiserum, conjugated normal rabbit serum or different antigens failed to react with the tissues.

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 Some properties of neutral-salt-soluble collagen. 2

1960 ◽  
Vol 76 (3) ◽  
pp. 463-471 ◽  
Author(s):  
J. H. Fessler
Keyword(s):  
Neutral Salt ◽  
Soluble Collagen

scholarly journals COLLAGEN METABOLISM IN OSTEOLATHYRISM IN CHICK EMBRYOS: SITE OF ACTION OF ß-AMINOPROPIONITRILE

1962 ◽  
Vol 116 (1) ◽  
pp. 45-54 ◽  
Author(s):  
J. Donald Smiley ◽  
Henry Yeager ◽  
Morris Ziff
Keyword(s):  
Specific Activity ◽  
Soluble Fraction ◽  
Specific Radioactivity ◽  
Collagen Fibers ◽  
Collagen Metabolism ◽  
Neutral Salt ◽  
Chick Embryos ◽  
Soluble Collagen ◽  
Site Of Action ◽  
Residue Fraction

Chick embryos were sacrificed at intervals after simultaneous injection of BAPN and proline-C14, the collagen separated into neutral salt-extractable and residue fractions, and total hydroxyproline and hydroxyproline specific radioactivity determined in each fraction. Extractable collagen, measured as hydroxyproline, increased markedly and had a higher specific activity in BAPN-treated embryos than in corresponding controls. Hydroxyproline of the residue collagen in the treated animals, however, had a lower specific activity. When proline-C14 was injected 24 hours prior to BAPN, the specific radioactivity of the soluble collagen of treated embryos was similar to that of controls, in spite of the fact that the specific activity of the residue fraction was higher than that of the soluble fraction at the time of BAPN administration. These results suggest that the increased amount of soluble collagen in lathyrism induced by administration of BAPN does not arise from the collagen insoluble prior to administration of the drug, but rather that BAPN acts by blocking the formation of mature collagen fibers, perhaps by preventing the formation of cross-linkages between α-collagen chains.

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