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Procollagen peptidase (EC 3.4.24.14, procollagen N-terminal peptidase, procollagen aminopeptidase, aminoprocollagen peptidase, aminoterminal procollagen peptidase, procollagen aminoterminal protease, procollagen N-terminal proteinase, type I/II procollagen N-proteinase, type III procollagen) is an endopeptidase involved in the processing of collagen.
Studies have shown that collagen production decreases by about 1% per year after the age of 20, emphasizing the significance of external support during this crucial phase of life. As the global co
Collagen (/ ˈ k ɒ l ə dʒ ə n /) is the main structural protein in the extracellular matrix of the connective tissues of many animals. It is the most abundant protein in mammals, [1] making up 25% to 35% of protein content. Amino acids are bound together to form a triple helix of elongated fibril [2] known as a collagen helix.
Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by homotrimers of collagen, type II, alpha 1 chains. It makes up 50% of all protein in cartilage and 85–90% of collagen of articular cartilage.
The CTX test measures for the presence and concentration of a crosslink peptide sequence of type I collagen, found, among other tissues, in bone. This specific peptide sequence relates to bone turnover because it is the portion that is cleaved by osteoclasts during bone resorption, and its serum levels are therefore proportional to osteoclastic ...
Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix. This makes the overall arrangement more sloppy with kinks. These two features cause the collagen to form in a sheet, the form of the basal lamina. Collagen IV is the more common usage, as opposed to the older terminology of "type-IV ...
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