hydroxylysine


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hydroxylysine

 [hi-drok″sĭ-li´sēn]
a naturally occurring amino acid.

hydroxylysine

(hī″drŏk-sĭl′ĭ-sĭn)
An amino acid found in collagen.
References in periodicals archive ?
In such cases, more adipose tissue is present and other more adipose or skin-related markers, such as hydroxylysine or hydroxyproline [32-33], could be included in the blood analysis.
Crosslinking of the collagenous materials with GTA involve the reaction of free amino groups of lysine or hydroxylysine amino acid residues of the polypeptide chains with the aldehyde groups (Fig.
The peak separation is >95% on common amino acids profile (up to 45 amino acids in a single run with Lithium systems), including Taurine, Ornithine, oxidized amino acids such as Cysteic acid and Methionine Sulfone, and hydroxylated amino acids such as Hydroxyproline and Hydroxylysine. There is a choice of two buffer systems available, both totally optimized for food and feedstuff analysis including an accelerated buffer system for high sample throughput labs.
Next, another key amino acid in the triple helix, lysine, is also hydroxylated, transforming it into hydroxylysine. This permits the cross-linking of the triple helices into tissue fibers and networks and completes the structure of collagen.
(2) The diagnosis was confirmed by decreased hydroxylysine residues in dermal collagen and decreased collagen lysl hydroxylase activity in their cultured skin fibroblasts.
Crosslinks are formed enzymatically among three specific amino acids (hydroxylysine or lysine residues) present within two adjacent but staggered collagen molecules.
For other targets, such as Lox, the connections between predictor and target gene were less clear, Lox is an extracellular and intracellular copper-containing enzyme that initiates cross-linking of collagen and elastin by catalyzing oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin.
Simple sugars may be bound to collagens at hydroxylysine residues by unique O-linkages (galactosyl-hydroxylysine and glucolylgalactosyl-hydroxylysine; Piez, 1984).
Two collagen-specific amino acids, hydroxyproline and hydroxylysine, are particularly elevated in the blood serum of rachitic individuals as a result of high bone turnover (VanderJagt et al.
Hyl/collagen HP/collagen (mol/mol) (mmol/mol) Fibroid tissues 57 [+ or -] 2.15 * 185.33 [+ or -] 13.7 * Myometrial tissues 28 [+ or -] 3.4 40.3 [+ or -] 3.7 HP + LP/collagen LP/collagen (mmol/mol) (mmol/mol) Fibroid tissues 15.7 [+ or -] 2.1 * 201 [+ or -] 12.5 * Myometrial tissues 25.9 [+ or -] 1.6 66.2 [+ or -] 2.3 HP/LP (mol/mol) Fibroid tissues 12.3 [+ or -] 2.4 * Myometrial tissues 1.6 [+ or -] 0.22 Table 3: Hydroxylysine (Hyl), hydroxylysylpyridinoline (HP), and lysylpyridinoline (LP) levels in small, medium, and large UF and their matched myometrial tissues.
Glutamate (1.43 g/100 g) was the most abundantly found and G-aminobutyric acid (0.01 g/100 g) and hydroxylysine (0.01 g/100 g) contents were the lowest ones.
BDDGE crosslinking involves the reaction of amine groups of lysine or hydroxylysine residues present in the collagen with epoxide groups of BDDGE molecules, resulting in formation of secondary amines.