Hydroxylysine in the N-terminal regions of the 1 - and 2 -chains of various collagens

The degree of hydroxylation of the lysine residue located in both alpha(1)- and alpha(2)-chains of collagen in the N-terminal, non-helical telopeptide region of the molecule has been determined in collagen from various sources after isolation of the peptides (alpha(1)- and alpha(2)-CB1) that contain...

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Bibliographic Details
Published in:Biochemical journal 1971-11, Vol.125 (2), p.433-437
Main Authors: Barnes, M J, Constable, B J, Morton, L F, Kodicek, E
Format: Article
Language:English
Subjects:
Animals
Chick Embryo
Chickens
Chromatography
Collagen - analysis
Cyanogen Bromide
Femur - analysis
Frontal Bone - analysis
Hydroxylysine - analysis
Lysine - analysis
Peptides - isolation & purification
Rats
Skin - analysis
Tail
Tendons - analysis
Tibia - analysis
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Summary:The degree of hydroxylation of the lysine residue located in both alpha(1)- and alpha(2)-chains of collagen in the N-terminal, non-helical telopeptide region of the molecule has been determined in collagen from various sources after isolation of the peptides (alpha(1)- and alpha(2)-CB1) that contain the lysine residue in question and are obtained by cyanogen bromide cleavage of collagen alpha(1)- and alpha(2)-chains respectively. As with collagen from chick tibia, bone collagens from rat tibia and femur and embryonic chick frontal bone, have a high degree of hydroxylation (approx. 50% or more) of the lysine residue in both alpha(1)- and alpha(2)-CB1 peptides. This is in contrast with the lack of hydroxylation of this residue in both alpha(1)- and alpha(2)-chains of all skin collagens so far examined. The presence of hydroxylysine in alpha(1)- and alpha(2)-CB1 peptides from tendon collagen is also indicated. In rat tail tendon collagen the amount of hydroxylation is only slight but in the much less soluble tendon collagen from embryonic chick leg tendons, approximately one-third of the lysine is hydroxylated.
ISSN:0264-6021
DOI:10.1042/bj1250433