The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen.

abstract

• Protocollagen, a non-hydroxylated form of collagen, was extracted with cold 0.1 N acetic acid from embryonic tendon cells incubated with ,-dipyridyl and the protein was purified by controlled proteolytic digestion. The resulting modified protocollagen was shown to consist of polypeptides the same size as 1 and 2 chains of collagen and had a thermal transition by optical rotation similar to collagen. The Tm however was 24, a value which was 15 lower than the Tm of an hydroxylated form of collagen from the same source. The results suggest that hydroxylated proline increases the thermal stability of collagen. 1973.

published proceedings

• Biochem Biophys Res Commun

altmetric score

• 9

author list (cited authors)

• Berg, R. A., & Prockop, D. J.

citation count

• 531

complete list of authors

• Berg, RA||Prockop, DJ

publication date

• January 1973

publisher

• Elsevier  Publisher

published in

• Biochemical and Biophysical Research Communications  Journal

keywords

• Animals
• Carbon Isotopes
• Chick Embryo
• Chromatography, Gel
• Chymotrypsin
• Collagen
• Culture Techniques
• Drug Stability
• Electrophoresis, Polyacrylamide Gel
• Hot Temperature
• Hydroxyproline
• Kinetics
• Protein Conformation
• Protein Denaturation
• Protein Precursors
• Skin
• Sodium Dodecyl Sulfate
• Tendons

Digital Object Identifier (DOI)

• 10.1016/0006-291x(73)90961-3

start page

• 115

end page

• 120

volume

• 52

issue

• 1

URL

• http://dx.doi.org/10.1016/0006-291x(73)90961-3