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 The effect of γ-irradiation on soluble collagen

1968 ◽  
Vol 107 (1) ◽  
pp. 29-34 ◽  
Author(s):  
R. J. Davidson ◽  
D. R. Cooper
Keyword(s):  
Conformational Changes ◽  
Irradiation Dose ◽  
Neutral Salt ◽  
Native Structure ◽  
Γ Irradiation ◽  
Peptide Bonds ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Principal Effect ◽  
Initial Effect

1. A study was made of the effect of γ-irradiation on the sub-unit composition, as well as the conformational changes taking place in cooled solutions of thermally denatured neutral-salt-soluble and acid-soluble 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 initial effect of γ-irradiation is the depolymerization of the dimers found in both neutral-salt-soluble and acid-soluble collagen. 4. The principal effect of γ-irradiation up to 10 Mrads is the fission of peptide bonds, yielding crystalline irradiation-resistant portions of the molecule incapable of associating to the native structure. 5. The effects of γ-irradiation on both neutral-salt-soluble and acid-soluble collagen are very similar and bear a close resemblance to the effects induced by ultraviolet irradiation.

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.

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

Extraction and Partial Characterization of Pepsin-Soluble Collagens from the Skin of Amiurus Nebulosus

2011 ◽  
Vol 236-238 ◽  
pp. 2926-2934 ◽  
Author(s):  
Li Li Chen ◽  
Li Zhao ◽  
Hua Liu ◽  
Run Feng Wu
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Alternative Source ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Sds Page ◽  
Skin Collagen ◽  
Maximal Yield ◽  
Pepsin Soluble Collagen

Pepsin-soluble collagen (PSC) was successfully extracted from the skin of Amiurus nebulosus. The skin of Amiurus nebulosus was immersed in 0.3 mol/L acetic acid (1: 20, m: V) for 6 h at 37°C, while pepsin was added, at a level of 5000U/g dosage of defatted skin. The maximal yield of the collagen was 97.44%, which was higher than that of acid-soluble collagen (ASC) at 62.05%. Some properties of pepsin-soluble collagens from the skin of Amiurus nebulosus were characterized. Amino acid composition and SDS-PAGE suggested that the collagen might be classified as type I collagen. Moreover, FTIR investigations showed the existence of helical arrangements in PSC of Amiurus nebulosus skin of collagen. There is a possibility to use Amiurus nebulosus skin collagen as an alternative source of collagen for industrial purposes and subsequently it may maximize the economical value of the fish.

scholarly journals Preparation and Characterization of Thermally Stable Collagens from the Scales of Lizardfish (Synodus macrops)

Marine Drugs ◽  
2021 ◽  
Vol 19 (11) ◽  
pp. 597
Author(s):  
Junde Chen ◽  
Guangyu Wang ◽  
Yushuang Li
Keyword(s):  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Type I ◽  
Salting Out ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Skin Collagen ◽  
Rat Tail

Marine collagen is gaining vast interest because of its high biocompatibility and lack of religious and social restrictions compared with collagen from terrestrial sources. In this study, lizardfish (Synodus macrops) scales were used to isolate acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC). Both ASC and PSC were identified as type I collagen with intact triple-helix structures by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and spectroscopy. The ASC and PSC had high amino acids of 237 residues/1000 residues and 236 residues/1000 residues, respectively. Thus, the maximum transition temperature (Tmax) of ASC (43.2 °C) was higher than that of PSC (42.5 °C). Interestingly, the Tmax of both ASC and PSC was higher than that of rat tail collagen (39.4 °C) and calf skin collagen (35.0 °C), the terrestrial collagen. Solubility tests showed that both ASC and PSC exhibited high solubility in the acidic pH ranges. ASC was less susceptible to the “salting out” effect compared with PSC. Both collagen types were nontoxic to HaCaT and MC3T3-E1 cells, and ASC was associated with a higher cell viability than PSC. These results indicated that ASC from lizardfish scales could be an alternative to terrestrial sources of collagen, with potential for biomedical applications.

scholarly journals Isolation and characterization of acid and pepsin soluble collagen extracted from sharpnose stingray (Dasyatis zugei) skin

Food Research ◽  
2020 ◽  
Vol 5 (3) ◽  
Author(s):  
T.Y. Ong ◽  
M.I. Shaik ◽  
N.M. Sarbon
Keyword(s):  
Helical Structure ◽  
Alternative Source ◽  
Soluble Collagen ◽  
Isolation And Characterization ◽  
Fibrous Network ◽  
Acid Soluble Collagen ◽  
Maximum Temperatures ◽  
Surface Morphologies ◽  
Pepsin Soluble Collagen

This study aimed to isolate and characterize the acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the skin of the sharpnose stingray (Dasyatis zugei). Isolated ASC and PSC were subjected to chemical and physical characterizations. The yield of PSC (34.84±1.26%) was significantly higher than that of ASC (20.48±4.41%) (p<0.05). There were no significant differences between ASC and PSC in terms of chemical composition (p>0.05). Both ASC and PSC were thermally stable at high temperatures, with denaturation temperatures of 24.1°C and 25.2°C, respectively, and maximum temperatures of 31.94±0.13°C and 31.79±0.23°C, respectively. Fourier transform infrared (FTIR) investigations showed the presence of triple helical structure with strong hydrogen bonding in both ASC and PSC. Meanwhile, both collagens were highly solubilized at acidic pH but at different optimal pH. The surface morphologies of ASC and PSC were loose and possessed slender, less uniform and irregular fibrous network structures with large and irregular pores observed between the fibrils. This finding showed that the alternative source of marine collagen possesses good physicochemical properties which highly potential for nutraceutical, pharmaceutical or cosmeceutical application.

scholarly journals Effect of compounds of the urea–guanidinium class on renaturation and thermal stability of acid-soluble collagen

1972 ◽  
Vol 127 (5) ◽  
pp. 855-863 ◽  
Author(s):  
A. E. Russell ◽  
D. R. Cooper
Keyword(s):  
Thermal Stability ◽  
Common Mechanism ◽  
Soluble Collagen ◽  
Activity Variation ◽  
Molar Activity ◽  
Acid Soluble Collagen ◽  
Skin Collagen ◽  
Thermal Stability Of ◽  
Calf Skin ◽  
Guanidinium Salts

The effects of guanidinium salts in decreasing the renaturation rate and lowering the thermal stability of acid-soluble calf-skin collagen have been compared with those of formamide and urea. With the exception of guanidinium sulphate at higher concentrations, no qualitative differences were apparent in the effects of these perturbants, which thus differed only in molar activity. Activity variation in the guanidinium salts reflected a net effect resulting from additivity of cation and anion contributions. As observed in other protein systems, lyotropic activity increased in the series formamide<urea<guanidinium ion, and in the guanidinium salts in the anion order fluoride<sulphate<chloride<bromide<nitrate<iodide. Low activities of guanidinium fluoride and sulphate were attributable to counter-effects of the anions, which acted as structural stabilizers. Changes in renaturation kinetics induced by either temperature or added perturbants appeared to conform with the Flory–Weaver model for the collagen transition. Additivity and non-specificity of the observed effects are discussed with particular reference to a common mechanism involving weak, non-saturated binding of perturbants at protein peptide groups.

scholarly journals The decomposition of soluble collagen by γ-irradiation

1969 ◽  
Vol 113 (2) ◽  
pp. 263-269 ◽  
Author(s):  
D. R. Cooper ◽  
A. E. Russell
Keyword(s):  
Irradiation Dose ◽  
Optical Rotation ◽  
Specific Rotation ◽  
Γ Irradiation ◽  
Soluble Collagen ◽  
Heating And Cooling ◽  
Reduced Viscosity ◽  
Acid Soluble Collagen ◽  
Freeze Dried ◽  
High Degree

1. The effect of γ-irradiation in the range 1 krad–10 Mrads on freeze-dried acid-soluble collagen was studied. 2. The specific-rotation and reduced-viscosity recoveries after heating and cooling of the irradiated collagen in solution showed a high degree of dependence on irradiation dose, with reduced viscosity showing significantly less recovery than specific rotation on increasing the irradiation dose. 3. The dependence of reduced viscosity on concentration was greatly decreased with increased doses of γ-irradiation. 4. The melting temperature measured by optical rotation also decreased as the irradiation dose was increased, and at low doses was distinctly biphasic. 5. Physical properties showed that the action of γ-irradiation up to 10 Mrads occurred in two distinct phases, with the early changes being extremely sensitive to irradiation dose. 6. The action of the γ-irradiation is discussed in terms of the structure of tropocollagen.

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