As we age, collagen production is reduced directly causing common problems such as joint pain, weak nails, dull hair, and a significant increase in the appearance of wrinkles. With new medical discoveries, we now have the ability to reintroduce natural collagen into our bodies. Around the age of 25 our bodies deplete their stores of collagen faster then they can produce them (typically at a rate of 1.5% per year). By the time most people have reached the age of 40, their body has completely stopped producing collagen. Not only will Collagen Natural products help restore your body’s supply of collagen but it will enable your body to produce its own. Formula q5-26 is made from 100% natural ingredients that contain no toxins, artificial colors, or fragrances. This is especially beneficial for those with sensitive skin and it protects the triple helix structure of the collagen proteins. Lactic acid is the only acid reaction, which does not endanger fiber spatial structure, but acting keratolically, it accelerates epidermis exfoliation. Natural Polish Collagen Formula q5-26 Ingredients: Dr. Maria Sadowska and Dr. Ilona Kolodzieiska, were the first to discover the specific and amazing benefits of collagen extracted from the Silver Carp, commonly known as the Balken Carp. They focused their methods from all fish by-products to extracting the collagen from the skin using an acidic polysaccharide derived from plant tissue. Their discoveries and techniques were further developed by Professor Josef Przybylski of The University Institute of Chemistry in Gdansk, Poland. He spearheaded a large scale research operation which discovered that specific filtering methods using fibrous silk filtration could be used to obtain triple helix structures in the large quantities necessary for cosmetic production. Collagen Natural contains collagen that is closely structured to human collagen and that is why it is easily absorbed into the skin. The proteins must be less than 350,000 molecular weight to be absorbed and the protein chains produced from carp for Collagen Natural are in the 250,000 to 310,000 range. Bovine or pig collagen cannot be absorbed through the skin and must be injected to be effective. Collagen Natural provides all the benefits of introducing new collagen without the painful procedures associated with cosmetic surgery. The results of this revolutionary skin care have amazed clinicians. You will immediately notice a tightening of the skin as the product begins to work. Fine lines disappear! Within 30 minutes of application, new collagen is introduced into the cells. Once absorbed, a mesh-like structure of protein is formed creating the building blocks for new collagen produced by the fibroblasts that bind moisture and lipofilic substances. Independent studies in Poland, the USA, and France verified results of studies using electron microscopes confirming the increased production of collagen by the fibroblasts. The result is an increase in mucine and derma thickness. The following collagen information provided by http://www.wikipedia.org: From the Greek for glue, kolla, the word collagen means “glue producer." Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, making up about 25% of the total protein content. It is one of the long, fibrous structural proteins whose functions are quite different from those of globular proteins such as enzymes; tough bundles of collagen called collagen fibers are a major component of the extracellular matrix that supports most tissues and gives cells structure from the outside, but collagen is also found inside certain cells. Collagen has great tensile strength, and is the main component of fascia, cartilage, ligaments, tendons, bone and teeth. Along with soft keratin, it is responsible for skin strength and elasticity, and its degradation leads to wrinkles that accompany aging. It strengthens blood vessels and plays a role in tissue development. It is present in the cornea and lens of the eye in crystalline form. Collagen has been widely used in cosmetic surgery, as a healing aid for burn patients for reconstruction of bone and a wide variety of dental, orthopedic and surgical purposes. The tropocollagen or "collagen molecule" subunit is a rod about 300 nm long and 1.5 nm in diameter, made up of three polypeptide strands, each of which is a left-handed helix, not to be confused with the commonly occurring alpha helix, which is right-handed. These three left-handed helices are twisted together into a right-handed coiled coil, a triple helix, a cooperative quaternary structure stabilized by numerous hydrogen bonds. Tropocollagen subunits spontaneously self-assemble, with regularly staggered ends, into even larger arrays in the extracellular spaces of tissues. There is some covalent crosslinking within the triple helices, and a variable amount of covalent crosslinking between tropocollagen helices, to form the different types of collagen found in different mature tissues — similar to the situation found with the α-keratins in hair. Collagen's insolubility was a barrier to study until it was found that tropocollagen from young animals can be extracted because it is not yet fully crosslinked. Collagen fibrils are collagen molecules packed into an organized overlapping bundle. Collagen fibers are bundles of fibrils. A distinctive feature of collagen is the regular arrangement of amino acids in each of the three chains of these collagen subunits. The sequence often follows the pattern Gly-X-Pro or Gly-X-Hyp, where X may be any of various other amino acid residues. Gly-Pro-Hyp occurs frequently. This kind of regular repetition and high glycine content is found in only a few other fibrous proteins, such as silk fibroin. 75-80% of silk is (approximately) -Gly-Ala-Gly-Ala- with 10% serine — and elastin is rich in glycine, proline, and alanine (Ala), whose side group is a small, inert methyl. Such high glycine and regular repetitions are never found in globular proteins. Chemically-reactive side groups are not needed in structural proteins as they are in enzymes and transport proteins. The high content of Pro and Hyp rings, with their geometrically constrained carboxyl and (secondary) amino groups, accounts for the tendency of the individual polypeptide strands to form left-handed helices spontaneously, without any intrachain hydrogen bonding. Because glycine is the smallest amino acid, it plays a unique role in fibrous structural proteins. In collagen, Gly is required at every third position because the assembly of the triple helix puts this residue at the interior (axis) of the helix, where there is no space for a larger side group than glycine’s single hydrogen atom. For the same reason, the rings of the Pro and Hyp must point outward. These two amino acids thermally stabilize the triple helix — Hyp even more so than Pro — and less of them is required in animals such as fish, whose body temperatures are low.
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