Reaction of the Human Anti-Gelatine Factor
with Gelatine from Different Species and with Collagen
Peptides

Wolff, I.; Timpl, R.

doi:10.1159/000467107

Cited by 1 publication

(1 citation statement)

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“…However, homologous sequences exist in these a-chains (Fietzek & Kuhn, 1976). Corroborating the results of Wolff & Timpl (1968), anti-gelatin factor did not distinguish between collagens obtained from different species. These observations indicate that the collagen sequences involved in the reaction are not highly mutable.…”

Section: Discussionmentioning

confidence: 71%

Identification of the sites in collagen α-chains that bind serum anti-gelatin factor (cold-insoluble globulin)

Dessau¹,

Adelmann²,

Timpl³

1978

Biochemical Journal

201

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Anti-gelatin factor was prepared from guinea-pig and human serum by affinity chromatography on denatured type-I collagen. As shown previously, this component is related to cold-insoluble globulin. It reacted with 125I-labelled denatured collagen, and the reaction could be inhibited by preincubation with unlabelled collagenous components. In the inhibition assay comparable activities were observed for native and denatured type-I, -II, -III and -IV collagens. There was also no difference in reactivity between collagens of different species. The reactive sites in the collagen alpha-chains were located by inhibition assays on distinct CNBr- and collagenase-derived peptides. The results obtained with fragments from alpha1(I)-, alpha2- and alpha1(II)-chains indicate that the most active region is located between positions 643 and 819 of the alpha1-chain. Lower activities were found for other regions of collagen and may indicate that the factor has the potential to interact with several sites in the alpha-chains. The present data agree with observations by Kleinman, McGoodwin & Klebe [Biochem. Biophys. Res. Commun. (1976) 72, 426-432] on the specificity of a serum factor promoting the attachment of fibroblasts to collagen.

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Section: Discussionmentioning

confidence: 71%