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 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 Differential anion effects on thermal stability of collagen in the dispersed and aggregated states

1974 ◽  
Vol 137 (3) ◽  
pp. 599-602 ◽  
Author(s):  
A. E. Russell
Keyword(s):  
Thermal Stability ◽  
Acid Solution ◽  
Thermal Transition ◽  
Dilute Solution ◽  
Dilute Acid ◽  
Dilute Acid Solution ◽  
Skin Collagen ◽  
Collagen Molecules ◽  
Thermal Stability Of ◽  
Calf Skin

The effects of KCNS and KI on thermal transition temperatures of calf skin collagen molecules in dilute acid solution and precipitated collagen fibrils from the same source were compared as a function of salt concentration and pH. The two salts produced qualitatively similar effects on each collagen form, but the response shown by single collagen molecules in dilute solution differed from that observed for molecular aggregates present in native-type fibrils.

Isolation and characterisation of acid- and pepsin-soluble collagen from the skin of Cervus korean TEMMINCK var. mantchuricus Swinhoe

2018 ◽  
Vol 58 (3) ◽  
pp. 585 ◽  
Author(s):  
Gaurav Lodhi ◽  
Yon-Suk Kim ◽  
Eun-Kyung Kim ◽  
Jin-Woo Hwang ◽  
Hyung-Sik Won ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Thermal Denaturation ◽  
Peptide Hydrolysis ◽  
Denaturation Temperature ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Thermal Denaturation Temperature ◽  
Skin Collagen ◽  
Pepsin Soluble Collagen ◽  
Calf Skin

Acid-soluble collagen and pepsin-soluble collagen were extracted from the skin of deer, Cervus korean TEMMINCK var. mantchuricus Swinhoe. The two types of collagen were then characterised using sodium dodecyl sulfate–polyacrylamide gel electrophoresis, amino acid composition analysis, peptide hydrolysis patterns, thermal denaturation temperature, differential scanning calorimetry, Fourier transform infrared spectroscopy, and nuclear magnetic resonance imaging. The yield of pepsin-soluble collagen (9.62%) was greater than that of acid-soluble collagen (2.24%), but both types of collagen showed similar electrophoretic patterns with each other and with calf skin collagen. The peptide hydrolysis pattern results suggested that calf skin collagen and pepsin-soluble collagen from deer skin may be similar in terms of their primary structure. The thermal denaturation temperature of acid-soluble collagen and pepsin-soluble collagen were 36.67°C and 36.44°C, respectively, and their melting temperatures were 110°C and 120°C, respectively, which suggest high thermal stability. Fourier transform infrared showed a triple helical structure and nuclear magnetic resonance confirmed the presence of ‘hydration’ water. These results provide a basis for large-scale production and further application as alternatives to other mammalian collagens.

scholarly journals Effect of pH on thermal stability of collagen in the dispersed and aggregated states (Short Communication)

1974 ◽  
Vol 139 (1) ◽  
pp. 277-280 ◽  
Author(s):  
Allan E. Russell
Keyword(s):  
Thermal Stability ◽  
Short Communication ◽  
Dilute Solution ◽  
Thermal Stabilities ◽  
Effect Of Ph ◽  
Soluble Collagen ◽  
Insoluble Collagen ◽  
Acid Soluble Collagen ◽  
Collagen Molecules ◽  
Thermal Stability Of

Thermal stabilities of mature insoluble collagen, salt-precipitated fibrils of acid-soluble collagen and acid-soluble collagen in solution were compared as a function of acid pH. Both insoluble and precipitated collagens showed large parallel destabilization with decrease in pH, whereas the intrinsic stability of individual collagen molecules in dilute solution was comparatively unaffected.

Thermal stability of calf skin collagen type I in salt solutions

1996 ◽  
Vol 1297 (2) ◽  
pp. 171-181 ◽  
Author(s):  
Regina Komsa-Penkova ◽  
Rumiana Koynova ◽  
Georgi Kostov ◽  
Boris G. Tenchov
Keyword(s):  
Thermal Stability ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Salt Solutions ◽  
Skin Collagen ◽  
Thermal Stability Of ◽  
Calf Skin

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 effects of certain glycols, substituted glycols and related organic solvents on the thermal stability of soluble collagen

1971 ◽  
Vol 125 (2) ◽  
pp. 599-604 ◽  
Author(s):  
G. J. Hart ◽  
A. E. Russell ◽  
D. R. Cooper
Keyword(s):  
Thermal Stability ◽  
Optical Rotation ◽  
Hydroxyl Group ◽  
Hydroxyl Groups ◽  
Thermal Transition ◽  
Denaturation Temperature ◽  
Rotation Measurement ◽  
Skin Collagen ◽  
Positional Isomerism ◽  
Thermal Stability Of

The effects of a number of related diols, substituted diols and glycerol on the thermal stability of acid-soluble calf skin collagen were investigated. Thermal transition temperatures were determined by optical rotation measurement. Short-chain diols with terminal hydroxyl groups, i.e. ethylene glycol and propane-1,3-diol, stabilized the protein at all accessible concentrations. Stabilization was also observed with glycerol and diethylene glycol. Higher homologues in the diol series produced various effects, as did hydroxyl-group positional isomerism. Monoalkyl substitution of diols progressively lowered the denaturation temperature of collagen. Results are discussed in relation to possible mechanisms of perturbant action.

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.

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