Hydroxyproline


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hydroxyproline

[hī¦dräk·sə′prō‚lēn]
(biochemistry)
C5H9O3N An amino acid that is essentially limited to structural proteins of the collagen type.

Hydroxyproline

 

4-hydroxy-2-pyrrolidinecarboxylic acid, a heterocyclic amino acid (in terms of chemical structure, an imino acid).

Hydroxyproline was first isolated from gelatin hydrolyzates in 1902 by E. Fischer. Because of the presence of two asymmetric carbon atoms per molecule, it has four optically active forms (L-, D-, allo-L-, and allo-D-hydroxyprolines) and two racemic forms. Natural L-hydroxyproline is a specific constituent of proteins in connective tissue, collagen and elastin (up to 13 percent), as well as of certain vegetable proteins; other proteins contain negligible amounts of L-hydroxyproline or none at all. Allo-L-hydroxypro-line was discovered in free form in sandalwood and is a component of toxic peptides in the death-cap. The formation of L-hydroxyproline in living cells is effected by hydroxylation of the proline bonded to the protein components (the O atom of the hydroxyl group is incorporated into hydroxyproline upon fixation of molecular O2). One of the products formed during the conversion of L-hydroxyproline in the organism is glutamic acid.

References in periodicals archive ?
They are often combined with other vitamins and ingredients such as Type 2 hydrolysates and glucosamine for joint health; for example, low molecular weight Bio Cell is combined with proline hydroxyproline and vitamin C for healthy skin and hair.
As hydroxyproline is a basic constituent of collagen structure, its content can serve as indicator of collagen synthesis.
Right lungs were excised for hydroxyproline determination via the chloramine-T spectro-photometric absorbance assay as previously described (Fattman et al.
In addition, hydroxyproline is involved in gel formation of nucleation zones via hydrogen bonding through its -OH group (Kittiphattanabawon et al.
Compared with Dahl + NS group, the contents of collagen-I, collagen-III, and hydroxyproline of renal tissue in Dahl + HS group were significantly increased (P < 0.
11] Reddy GK, Enwemeka CS, "A simplified method for the analysis of hydroxyproline in biological tissues," Clinical Biochemistry, vol.
2007) who reported that the hydroxyproline and proline contents of silver carp are slightly higher than those of a carp.
Hydroxyproline level which is the main marker of the collagen amount was used for assessment of collagen levels in the wound.
However mandible showed greater hydroxyproline content and lower glycine content than other spectra.

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