Addition of mannose to both the amino- and carboxy-terminal properties of type II procollagen occurs without formation of a triple helix. Academic Article

abstract

• Matrix-free cells obtained from chick embryo cartilage were incubated in the presence of ,-dipyridyl and radioactive mannose in order to examine the incorporation of mannose into the propeptide extensions of Type II procollagen. Cell proteins were digested with bacterial collagenase and the digests were examined by polyacrylamide gel electrophoresis. Radioactive mannose was found in fragments from both the N- and C-propeptides, and therefore the results provided the first indication that both these propeptides of Type II procollagen contain mannose. The results also supported previous indications that addition of carbohydrate to the propeptides of procollagen does not require folding of the collagen domain into a triple helix. 1978.

published proceedings

• Biochem Biophys Res Commun

altmetric score

• 3

author list (cited authors)

• Guzman, N. A., Graves, P. N., & Prockop, D. J.

citation count

• 26

complete list of authors

• Guzman, NA||Graves, PN||Prockop, DJ

publication date

• January 1978

publisher

• Elsevier  Publisher

published in

• Biochemical and Biophysical Research Communications  Journal

keywords

• Animals
• Cartilage
• Chick Embryo
• Macromolecular Substances
• Mannose
• Procollagen
• Proline
• Tendons

Digital Object Identifier (DOI)

• 10.1016/0006-291x(78)90760-x

start page

• 691

end page

• 698

volume

• 84

issue

• 3

URL

• http://dx.doi.org/10.1016/0006-291x(78)90760-x