tropocollagen


Also found in: Dictionary, Medical, Wikipedia.
Related to tropocollagen: collagen fibers

tropocollagen

[¦träp·ō′kal·ə·jən]
(biochemistry)
The fundamental units of collagen fibrils.
References in periodicals archive ?
This involves the formation of pro-alpha chains, preprocollagen, procollagen, and tropocollagen fibrils and finally in the extracellular space copper-dependent lysyl oxidases (LOX) enzymatically create the intramolecular and intermolecular cross-links that form the mature collagen fibrils.
The authors show that, after delivery, the fast degeneration of the uterus results in fragmentation of tropocollagen by collagenolytic enzymes releasing actin, myosin, and their metabolites; these antibodies are formed against actin and cross-react with the myocardium.
(2) in ER [right arrow] preprocollagen, (3) ER Lumen [right arrow] signal peptides cleaved; proline and lysine hydroxylation, 2 pro-alpha1 and 1 pro-alpha2 chains [right arrow] Type I procollagen, triple helix formed [right arrow] (4) in Golgi packaged and secreted [right arrow] (5) outside cell propeptides cleaved [right arrow] tropocollagen fibrils formed, (6) lysyl oxidase creates intramolecular and intermolecular cross-links.
Its organic phase is composed of type I collagen, which is a fibrous insoluble protein formed from tropocollagen molecules, which in turn are composed of three coiled polypeptide chains linked by hydrogen bonds that make them compact providing the tissue with strength.
According to Cardium, its FDA-cleared Excellagen is an aseptically-manufactured, quaternary fibrillar Type I bovine collagen homogenate that is configured into a staggered array of three-dimensional, triple helical, telopeptide-deleted, tropocollagen molecules.
A similar mechanism of hardening and thickening of collagen fibers has been shown in corneal aging and is related to active glycosylation of age-dependent tropocollagen molecules [6].
Osteoblasts produce tropocollagen, which is a polymerized form of collagen and synthesize alkaline phosphatase (AP).
In salmons with JD type I and II collagen fibers decreased and III (forming fine fibers), increased specimens with vitamin C deficiency have [partial derivative] chains in the tropocollagen molecules unable to form estable loops to form fibrils.
The determined IR absorption ratio 1235/1450 [cm.sup.-1] was 1.1, suggesting that tropocollagen triple helix secondary structure was preserved.