Titre : |
The non-collagenous proteins of skin - Their characterisation and significance in leather processing |
Type de document : |
texte imprimé |
Auteurs : |
G. A. Balian, Auteur ; J. H. Bowes, Auteur |
Année de publication : |
1970 |
Article en page(s) : |
p. 171-182 |
Note générale : |
Bibliogr. |
Langues : |
Anglais (eng) |
Catégories : |
Acides aminés Les acides aminés (ou aminoacides) sont une classe de composés chimiques possédant deux groupes fonctionnels : à la fois un groupe carboxyle –COOH et un groupe amine –NH2. Parmi ceux-ci, les acides α-aminés se définissent par le fait que leur groupe amine est lié à l'atome de carbone adjacent au groupe acide carboxylique (le carbone α), ce qui leur confère la structure générique H2N–CHR–COOH, où R représente la chaîne latérale, qui identifie l'acide α-aminé.
Les acides α-aminés jouent un rôle fondamental en biochimie comme constituants élémentaires des protéines : ils polymérisent en formant des liaisons peptidiques qui aboutissent à de longues chaînes macromoléculaires appelées peptides. Caractérisation Cuirs et peaux de veaux Extraction (chimie) Protéines
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Index. décimale : |
675 Technologie du cuir et de la fourrure |
Résumé : |
The composition of the skin and the variations in the relative amounts of collagen and non-collagenous proteins in the skin with the type of animal, age and nutritional level are considered.
The non-collagenous protein shave been divided into four fractions on the basis of solubility and ease of extraction from skin. About 30% of the non-collagenous protein is extracted by phosphate buffer at pH 9.0 and by neutral salt solutions, a further "à ù by dilute alkali, pH 12.5, and the remaining 30% or so remains in association with the insoluble collagen. Ten to twenty per cent non-collagenous protein dissolves in acetic acid together with acid-soluble collagen.
The non-collagenous protein extracted by phosphate buffer, dilute alkali and acetic acid have been analysed for amino acid composition and examined by ion exchange and molecular sieve chromatography and acrylamide gel electrophoresis. The protein extracted by phosphate buffer has been shown to consist primarily of plasma proteins and is considered to arise from the blood supply and no have no function specific to skin.
The non-collagenous proteins extracted by acid and alkali differ in amino acid composition. Each canbe separated into a major and several minor components by acrylamide gel electrophoresis but few, if any, of these appear to be common to both extracts. The major component of the alkaline extract if of high molecular weight and is closely associated with the collagen. It represents a high proportion of the total non-collagenous protein of skin. The acid-soluble fraction is also closely associated with the collagen ; it contains an excess of acidic residues and is probably bound to the collagen by electrostatic forces.
The results as a whole demonstrate that thematrix of skin consists of a complex system of non-fibrous proteins, some of which are difficult to remove from association with collagen and vice versa. Their possible function in the stabiilisation of skin structure is examined.
These findings and recent advances in our knowledge of the structure and properties of collagen are discussed in relation to leather processing. |
Note de contenu : |
- Composition of skin
- Characterisation of the non-collegenous protein : Extraction - Alkaline extract - Acetic acid extracts - Insoluble protein
- Function of the non-collagenous proteins
- Implications in leather processing
- Table 1 : Protein extracted from calf skin - Percentage of total skin protein
- Table 2 : Amino acid composition of non-collagenous protein fractions extracted from calf skin |
En ligne : |
https://drive.google.com/file/d/1hIXcYHobRfD93QNnMdzYjNzz-3nDaEIN/view?usp=drive [...] |
Format de la ressource électronique : |
Pdf |
Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=37002 |
in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 54, N° 5 (05/1970) . - p. 171-182