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Cosmetic Ingredients Collagen CAS 9064-67-9 

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Place of Origin: Sichuan, China (Mainland) 
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Means of Transport: Ocean,Land,Air
Delivery Date: within 7 days
CAS No.: 9064-67-9
Molecular Formula: C4H6N2O3R2.(C7H9N2O2R)n
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Brand Name: MOSINTER
Brand: MOSINTER

Collagen is the main structural protein of the various connective tissues in animals.

Collagen (CAS: 9064-67-9)


Item

Index

Molecular Formula

C4H6N2O3R2.(C7H9N2O2R)n

Solubility

H2O: 5 mg/mL, hazy, colorless and viscous

Storage   Condition

2-8°C


Collagen is the main structural protein of the various connective tissues in animals. (The name collagen comes from the Greek kolla meaning glue and suffix -gendenoting producing.) As the main component of connective tissue, it is the most abundant protein in mammals, making up from 25% to 35% of the whole-body protein content. Collagen, in the form of elongated fibrils, is mostly found in fibrous tissues such as tendons, ligaments and skin, and is also abundant in corneas, cartilage, bones, blood vessels, the gut, and intervertebral discs. The fibroblast is the most common cell that creates collagen.

In muscle tissue, it serves as a major component of the endomysium. Collagen constitutes one to two percent of muscle tissue, and accounts for 6% of the weight of strong, tendinous muscles. Gelatin, which is used in food and industry, is collagen that has been irreversibly hydrolyzed.


Chemistry

Collagen is composed of a triple helix, which generally consists of two identical chains (α1) and an additional chain that differs slightly in its chemical composition (α2). The amino acid composition of collagen is atypical for proteins, particularly with respect to its high hydroxyproline content. The most common motifs in the amino acid sequence of collagen are glycine-proline-X and glycine-X-hydroxyproline, where X is any amino acid other than glycine, proline or hydroxyproline. The average amino acid composition for fish and mammal skin is given.


Amino acids

Collagen has an unusual amino acid composition and sequence:

  • Glycine is found at almost every third residue.

  • Proline makes up about 17% of collagen.

  • Collagen contains two uncommon derivative amino acids not directly inserted during translation. These amino acids are found at specific locations relative to glycine and are modified post-translationally by different enzymes, both of which require vitamin C as a cofactor.

  • Hydroxyproline derived from proline

  • Hydroxylysine derived from lysine - depending on the type of collagen, varying numbers of hydroxylysines are glycosylated (mostly having disaccharidesattached).

  • Cortisol stimulates degradation of (skin) collagen into amino acids

    Collagen I formation

    Most collagen forms in a similar manner, but the following process is typical for type I:

    • Inside the cell

    • Two types of alpha helices are formed during translation on ribosomes along the rough endoplasmic reticulum (RER): alpha-1 and alpha-2 helices. These form peptide chains (known as preprocollagen) have registration peptides on each end and a signal peptide.

    • Polypeptide chains are released into the lumen of the RER.

    • Signal peptides are cleaved inside the RER and the chains are now known as pro-alpha chains.

    • Hydroxylation of lysine and proline amino acids occurs inside the lumen. This process is dependent on ascorbic acid (vitamin C) as a cofactor.

    • Glycosylation of specific hydroxylysine residues occurs.

    • Triple ɣ helical structure is formed inside the endoplasmic reticulum from each two alpha-1 chains and one alpha-2 chain.

    • Procollagen is shipped to the Golgi apparatus, where it is packaged and secreted by exocytosis.

    • Outside the cell

    • Registration peptides are cleaved and tropocollagen is formed by procollagen peptidase.

    • Multiple tropocollagen molecules form collagen fibrils, via covalent cross-linking (aldol reaction) by lysyl oxidase which links hydroxylysine and lysine residues. Multiple collagen fibrils form into collagen fibers.

    • Collagen may be attached to cell membranes via several types of protein, including fibronectin and integrin.


    Synthetic pathogenesis

    Vitamin C deficiency causes scurvy, a serious and painful disease in which defective collagen prevents the formation of strong connective tissue. Gums deteriorate and bleed, with loss of teeth; skin discolors, and wounds do not heal. Prior to the 18th century, this condition was notorious among long-duration military, particularly naval, expeditions during which participants were deprived of foods containing vitamin C.

    An autoimmune disease such as lupus erythematosus or rheumatoid arthritis may attack healthy collagen fibers.

    Many bacteria and viruses secrete virulence factors, such as the enzyme collagenase, which destroys collagen or interferes with its production.


    Uses

    Collagen has a wide variety of applications, from food to medical. For instance, it is used in cosmetic surgery and burns surgery. It is widely used in the form of collagen casings for sausages, which are also used in the manufacture of musical strings.

    If collagen is subject to sufficient denaturation, e.g. by heating, the three tropocollagen strands separate partially or completely into globular domains, containing a different secondary structure to the normal collagen polyproline II (PPII), e.g. random coils. This process describes the formation of gelatin, which is used in many foods, including flavored gelatin desserts. Besides food, gelatin has been used in pharmaceutical, cosmetic, and photography industries. From a nutritional point of view, collagen and gelatin are a poor-quality sole source of protein since they do not contain all the essential amino acids in the proportions that the human body requires—they are not 'complete proteins' (as defined by food science, not that they are partially structured). Manufacturers of collagen-based dietary supplements claim that their products can improve skin and fingernail quality as well as joint health. However, mainstream scientific research has not shown strong evidence to support these claims.[citation needed] Individuals with problems in these areas are more likely to be suffering from some other underlying condition (such as normal aging, dry skin, arthritis etc.) rather than just a protein deficiency.

    From the Greek for glue, kolla, the word collagen means "glue producer" and refers to the early process of boiling the skin and sinews of horses and other animals to obtain glue. Collagen adhesive was used by Egyptians about 4,000 years ago, and Native Americans used it in bows about 1,500 years ago. The oldest glue in the world, carbon-dated as more than 8,000 years old, was found to be collagen—used as a protective lining on rope baskets and embroidered fabrics, and to hold utensils together; also in crisscross decorations on human skulls. Collagen normally converts to gelatin, but survived due to dry conditions. Animal glues are thermoplastic, softening again upon reheating, and so they are still used in making musical instruments such as fineviolins and guitars, which may have to be reopened for repairs—an application incompatible with tough, synthetic plastic adhesives, which are permanent. Animal sinews and skins, includingleather, have been used to make useful articles for millennia.

    Gelatin-resorcinol-formaldehyde glue (and with formaldehyde replaced by less-toxic pentanedial and ethanedial) has been used to repair experimental incisions in rabbit lungs.

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