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A transport form of collagen from embryonic tendon: electron microscopic demonstration of an NH 2 -terminal extension and evidence suggesting the presence of cystine in the molecule (chick embryo-tropocollagen-gel filtration).
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 1972 Jan; Vol. 69 (1), pp. 60-4. - Publication Year :
- 1972
-
Abstract
- When cells were isolated from chickembryo tendons and incubated in vitro for 2-6 hr, essentially all the newly-synthesized collagen was recovered from the incubation medium as a transport form larger than tropocollagen. Experiments in which cells were incubated with [(14)C]cystine suggested that the transport form contained cystine and that it was, in part, stabilized by disulfide bonds. Electron microscopy of segment-long-spacing aggregates prepared from the transport form of collagen showed that the native molecule differed from tropocollagen in that it had an extension of about 13 nm (130 A) at the NH(2)-terminal end.
- Subjects :
- Ammonium Sulfate
Animals
Anura
Biological Transport
Carbon Isotopes
Carrier Proteins analysis
Carrier Proteins metabolism
Chick Embryo
Chromatography, Gel
Collagen isolation & purification
Detergents
Microbial Collagenase
Microscopy, Electron
Pepsin A
Proline
Protein Conformation
Sulfates
Tropocollagen biosynthesis
Tropocollagen isolation & purification
Trypsin
Collagen biosynthesis
Cystine isolation & purification
Tendons metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0027-8424
- Volume :
- 69
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 4333046
- Full Text :
- https://doi.org/10.1073/pnas.69.1.60