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PMID: 656467 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Isolation of purified insoluble aortic collagen.

Biochimica et biophysica acta ·Vol. 534 ·No. 1 ·1978-05-24 ·Pages 64-72

Faris B, Moscaritolo R, Levine A, Snider R, Goldstein R, Franzblau C

Abstract

The chemistry of collagen from major blood vessels, such as the aorta, is poorly defined because of problems encountered in solubilization techniques. Normal extraction of calf aorta with acetic acid and/or pepsin does not yield significant quantities of collagen. However, treatment of the aorta with purified pancreatic elastase results in a residue containing a significant portion of the collagen. The amino acid analysis, the acrylamide gel electrophoretic patterns and the electron micrographs of this residue display characteristics consistent with relatively pure collagen. Using this purified collagen preparation approximately 90% of the collagenous material present can be solubilized by pepsin treatment.

MeSH Terms
Amino Acids/analysis Animals Aorta/analysis Cattle Collagen/analysis,isolation & purification Electrophoresis, Polyacrylamide Gel Hydroxyproline/analysis Pancreatic Elastase/metabolism Solubility
Chemicals
Amino Acids Collagen Pancreatic Elastase Hydroxyproline
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Faris B
Moscaritolo R
Levine A
Snider R
Goldstein R
Franzblau C
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1978-05-24
Pages
64-72
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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