scholarly journals THERMAL DENATURATION OF SOLUBLE CALF-SKIN COLLAGEN

1965 ◽  
Vol 95 (2) ◽  
pp. 350-353 ◽  
Author(s):  
GR TRISTRAM ◽  
J WORRALL ◽  
DC STEER
Keyword(s):  
Thermal Denaturation ◽  
Skin Collagen ◽  
Calf Skin

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 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

scholarly journals Completion of the amino acid sequence of the α1 chain from type I calf skin collagen. Amino acid sequence of α1(I)B8

1983 ◽  
Vol 215 (1) ◽  
pp. 183-189 ◽  
Author(s):  
R W Glanville ◽  
D Breitkreutz ◽  
M Meitinger ◽  
P P Fietzek
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Type I ◽  
Amino Acid Sequence Analysis ◽  
Complete Amino Acid Sequence ◽  
Skin Collagen ◽  
Arginine Residues ◽  
Calf Skin

The complete amino acid sequence of the 279-residue CNBr peptide CB8 from the alpha 1 chain of type I calf skin collagen is presented. It was determined by sequencing overlapping fragments of CB8 produced by Staphylococcus aureus V8 proteinase, trypsin, Endoproteinase Arg-C and hydroxylamine. Tryptic cleavages were also made specific for lysine by blocking arginine residues with cyclohexane-1,2-dione. This completes the amino acid sequence analysis of the 1054-residues-long alpha (I) chain of calf skin collagen.

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