PMID: 6409498May 1, 1983Paper

Extraction, isolation and characterization of neutral salt soluble type V collagen from fetal calf skin

Collagen and Related Research
S F Elstow, J B Weiss

Abstract

Collagen was extracted with neutral salt solution and examined for the presence of type V collagen. A fraction which was insoluble in both 0.02 M Na2HPO4, pH 9.2 and phosphate-buffered saline (PBS) pH 7.2 at 4 degrees C contained both alpha 1(V)- and alpha 2(V)-chains demonstrated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, diethylaminoethyl cellulose ion exchange chromatography, amino acid analysis and segment long spacing (SLS) crystallites. SLS crystallites showed a globular N-terminal extension peptide attached to the type V collagen monomer. Ion exchange chromatography also demonstrated the presence of a third, minor component, which was identified as the alpha 3(V)-chain. In certain extractions, components corresponding to the partially processed procollagen chains of type V collagen were also observed.

References

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Citations

Dec 1, 1984·Collagen and Related Research·C L MainardiJ M Seyer
Jun 1, 1985·Collagen and Related Research·E Adachi, T Hayashi
Apr 1, 1987·Collagen and Related Research·E Adachi, T Hayashi
Oct 23, 1998·Journal of Medical Genetics·A J RichardsN P Burrows
Nov 4, 2000·Connective Tissue Research·K InkinenJ Ahonen
Jan 1, 1988·Connective Tissue Research·J J CreelyM A Haralson
Mar 1, 1987·The Journal of Investigative Dermatology·D T WoodleyR A Briggaman
Sep 1, 1988·The Journal of Investigative Dermatology·Y HashimotoT Hayakawa
Jul 1, 1995·Matrix Biology : Journal of the International Society for Matrix Biology·A FichardF Ruggiero

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