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.

hydroxylysine

a naturally occurring amino acid.
References in periodicals archive ?
Measurement of hydroxylysine glucosides in urine and its application to spinal cord injury.
Hydroxylysine and hydroxyproline residues are present and both may be glycolated with simple sugars bound to hydroxylysine (Simpson, 1984).
The amino acid composition of the hydrolysates of all the blobs consists of about 30% glycine residues along with some hydroxyproline and hydroxylysine residues.
Bone resorption markers galactosyl hydroxylysine, pyridinium crosslinks, and hydroxyproline compared.
Although neither hydroxylysine nor hydroxyproline concentrations were determined, the amino acid composition suggested that the St.
Briefly, the Matsumura protocol consists of calculating the sum of each of the hydrophobic (valine, methionine, leucine, isoleucine, tyrosine, and phenylalanine), hydroxylated (hydroxyproline, threonine, serine, tyrosine, and hydroxylysine), and polar (aspartate, glutamate, hydroxylysine, lysine, histidine, ornithine, and arginine) amino acid residues per 1000 in the collagen hydrolysate.
We have shown previously (6-8) that this is also true for the urinary excretion of two collagen breakdown products, galactosyl hydroxylysine (Gal-Hyl) [4] and deoxypyridinoline (DPD).
9% for 1-methylhistidine to 17% for arginine, with the exception of hydroxylysine (22%).
Type 1 collagen, rich in the amino acid hydroxyproline, has a triple helix structure, with strands connected by cross-links between lysine or hydroxylysine residues that join the nonhelical amino- and carboxy-terminal ends of one collagen molecule to the helical portion of an adjacent molecule (1).
The most sensitive and specific markers of bone resorption have been based on measurement of urinary analytes, such as deoxypyridinoline (Dpd), [1] telopeptide fragments of type I collagen, and galactosyl hydroxylysine (1).
Trifunctional pyridinium cross-links--pyridinoline (Pyd) or deoxypyridinoline (Dpd)--form between hydroxylysine or lysine residues at the C- and N-telopeptide ends of one collagen molecule and the helical portion of a neighboring molecule during collagen maturation [2].