The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Collagen Made of Extended alpha-Chains, Procollagen, in Genetically-Defective Dermatosparaxic Calves
Abstract
Collagen has been extracted from the skin of dermatosparaxic calves and fractionated by acrylamide-gel electrophoresis and CM-cellulose chromatography. This collagen contains in large proportion two additional types of α-chains, P-α1 and P-α2. The first, P-α1, ressembles α1, of a collagen extracted from the skin of a normal calf in its amino-acid composition but its molecular weight is 10% larger. The second, P-α2, is similar to a normal α2 in its amino-acid composition but its molecular weight is increased by 5%. The abnormal α-chains contain six to eight half cystine residues in p-α1 and one in p-α2. As seen under the electron microscope on segment long spacing, the dermatosparaxic collagen is 25 nm larger than the normal collagen and the in creased length results from extension of the polypeptide chain at the N-terminal extremity of the molecules. Although the collagen is less extractable from the dermatosparaxic skin than from the normal skin and dimers and other polymers of the abnormal α-chains are observed, the dermatosparaxic collagen does not, in vitro, form fibrils of normal stability. Since an enzyme activity which can excise the N-terminal extension peptide of the dermatosparaxic collagen has been identified in extracts of normal skin but is absent in the dermatosparaxic animals, it is suggested that the dermatosparaxic collagen is a form of “procollagen”, from which all or a part of these peptides have not been removed and that such peptides function as coordinators in the post synthesis assembly of the collagen α-chains.
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Cites
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Some Properties of the Products of Reaction of Tadpole Collagenase with Collagen*
Sakai, T., & Gross, J. (1967) · Biochemistry · doi:10.1021/bi00854a021 · Cited by 247
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Layman, D. L., McGoodwin, E. B., & Martin, G. R. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.2.454 · Cited by 239
Evidence for Procollagen, a Biosynthetic Precursor of Collagen
Bellamy, G., & Bornstein, P. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.6.1138 · Cited by 193
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Cited by
Collagen fibrillogenesis in vitro: interaction of types I and V collagen regulates fibril diameter
Birk, D. E., Fitch, J. M., Babiarz, J. P., Doane, K. J., & Linsenmayer, T. F. (1990) · Journal of Cell Science · doi:10.1242/jcs.95.4.649 · Cited by 596
Biochemical characteristics and biological significance of the genetically-distinct collagens
Miller, E. J. (1976) · Molecular and Cellular Biochemistry · doi:10.1007/bf01731779 · Cited by 462
Weinstock, M., & Leblond, C. P. (1974) · The Journal of Cell Biology · doi:10.1083/jcb.60.1.92 · Cited by 377
Colige, A., Sieron, A. L., Li, S.-W., Schwarze, U., Petty, E., Wertelecki, W., Wilcox, W., Krakow, D., Cohn, D. H., Reardon, W., et al. (1999) · The American Journal of Human Genetics · doi:10.1086/302504 · Cited by 370
Self-citationThe Ehlers–Danlos syndromes, rare types
Brady, A. F., Demirdas, S., Fournel‐Gigleux, S., Ghali, N., Giunta, C., Kapferer‐Seebacher, I., Kosho, T., Mendoza‐Londono, R., Pope, M. F., Rohrbach, M., et al. (2017) · American Journal of Medical Genetics Part C Seminars in Medical Genetics · doi:10.1002/ajmg.c.31550 · Cited by 258
Metadata
- Authors
- Lenaers, A., Nusgens, B. V., LapiERE, C. M., & Ansay, M.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1971-12
- Volume
- 23
- Issue
- 3
- Pages
- 533-543
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W2009399173
- Cited by
- 295
- References
- 14
- FWCI
- 19.12
- Type
- journal article
- Language
- en
- Open access
- closed
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- Lenaers, A., Nusgens, B. V., LapiERE, C. M., & Ansay, M. (1971). Collagen Made of Extended alpha-Chains, Procollagen, in Genetically-Defective Dermatosparaxic Calves. European Journal of Biochemistry. https://doi.org/10.1111/j.1432-1033.1971.tb01651.x
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