Abstract
The complete amino acid sequence of the 279-residue CNBr peptide CB8 from the alpha 1 chain of type I calf skin collagen is presented. It was determined by sequencing overlapping fragments of CB8 produced by Staphylococcus aureus V8 proteinase, trypsin, Endoproteinase Arg-C and hydroxylamine. Tryptic cleavages were also made specific for lysine by blocking arginine residues with cyclohexane-1,2-dione. This completes the amino acid sequence analysis of the 1054-residues-long alpha (I) chain of calf skin collagen.
Full text
PDF






Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Balian G., Click E. M., Bornstein P. Structure of rat skin collagen 1-CB8. Amino acid sequence of the hydroxylamine-produced fragment HA1. Biochemistry. 1971 Nov 23;10(24):4470–4478. doi: 10.1021/bi00800a019. [DOI] [PubMed] [Google Scholar]
- Balian G., Click E. M., Hermodson M. A., Bornstein P. Structure of rat skin collagen alpha 1-CBB. Amino acid sequence of the hydroxyl amine-produced fragment HA2. Biochemistry. 1972 Sep 26;11(20):3798–3806. doi: 10.1021/bi00770a020. [DOI] [PubMed] [Google Scholar]
- Bornstein P. Structure of alpha-1-CB8, a large cyanogen bromide produced fragment from the alpha-1 chain of rat collagen. The nature of a hydroxylamine-sensitive bond and composition of tryptic peptides. Biochemistry. 1970 Jun 9;9(12):2408–2421. doi: 10.1021/bi00814a004. [DOI] [PubMed] [Google Scholar]
- Fietzek P. P., Kühn K. The covalent structure of collagen: amino-acid sequence of the cyanogen-bromide peptides alpha1-CB2, alpha1-CB4 and alpha1-CB5 from calf-skin collagen. Eur J Biochem. 1975 Mar 3;52(1):77–82. doi: 10.1111/j.1432-1033.1975.tb03974.x. [DOI] [PubMed] [Google Scholar]
- Fietzek P. P., Rexrodt F. W., Hopper K. E., Kühn K. The covalent structure of collagen. 2. The amino-acid sequence of alpha1-CB7 from calf-skin collagen. Eur J Biochem. 1973 Oct 5;38(2):396–400. doi: 10.1111/j.1432-1033.1973.tb03072.x. [DOI] [PubMed] [Google Scholar]
- Fietzek P. P., Rexrodt F. W., Wendt P., Stark M., Kühn K. The covalent structure of collagen. Amino-acid sequence of peptide 1-CB6-C2. Eur J Biochem. 1972 Oct 17;30(1):163–168. doi: 10.1111/j.1432-1033.1972.tb02083.x. [DOI] [PubMed] [Google Scholar]
- Fietzek P. P., Wendt P., Kell I., Kühn K. The covalent structure of collagen: amino acid sequence of 1-CB3 from calf skin collagen. FEBS Lett. 1972 Oct 1;26(1):74–76. doi: 10.1016/0014-5793(72)80545-3. [DOI] [PubMed] [Google Scholar]
- Henkel W., Glanville R. W. Covalent crosslinking between molecules of type I and type III collagen. The involvement of the N-terminal, nonhelical regions of the alpha 1 (I) and alpha 1 (III) chains in the formation of intermolecular crosslinks. Eur J Biochem. 1982 Feb;122(1):205–213. doi: 10.1111/j.1432-1033.1982.tb05868.x. [DOI] [PubMed] [Google Scholar]
- Highberger J. H., Corbett C., Dixit S. N., Yu W., Seyer J. M., Kang A. H., Gross J. Amino acid sequence of chick skin collagen alpha 1(I)-CB8 and the complete primary structure of the helical portion of the chick skin collagen alpha 1(I) chain. Biochemistry. 1982 Apr 27;21(9):2048–2055. doi: 10.1021/bi00538a011. [DOI] [PubMed] [Google Scholar]
- Hofmann H., Fietzek P. P., Kühn K. Comparative analysis of the sequences of the three collagen chains alpha 1(I), alpha 2 and alpha 1(III) Functional and genetic aspects. J Mol Biol. 1980 Aug 15;141(3):293–314. doi: 10.1016/0022-2836(80)90182-5. [DOI] [PubMed] [Google Scholar]
- Hofmann H., Fietzek P. P., Kühn K. The role of polar and hydrophobic interactions for the molecular packing of type I collagen: a three-dimensional evaluation of the amino acid sequence. J Mol Biol. 1978 Oct 25;125(2):137–165. doi: 10.1016/0022-2836(78)90342-x. [DOI] [PubMed] [Google Scholar]
- Hörlein D., Fietzek P. P., Wachter E., Lapière C. M., Kühn K. Amino acid sequence of the aminoterminal segment of dermatosparactic calf-skin procollagen type I. Eur J Biochem. 1979 Aug 15;99(1):31–38. doi: 10.1111/j.1432-1033.1979.tb13227.x. [DOI] [PubMed] [Google Scholar]
- Patthy L., Smith E. L. Reversible modification of arginine residues. Application to sequence studies by restriction of tryptic hydrolysis to lysine residues. J Biol Chem. 1975 Jan 25;250(2):557–564. [PubMed] [Google Scholar]
- Rauterberg J., Fietzek P., Rexrodt F., Becker U., Stark M., Kühn K. The amino acid sequence of the carboxyterminal nonhelical cross link region of the alpha 1 chain of calf skin collagen. FEBS Lett. 1972 Mar;21(1):75–79. doi: 10.1016/0014-5793(72)80167-4. [DOI] [PubMed] [Google Scholar]
- Rauterberg J., Kühn K. Acid soluble calf skin collagen. Characterization of the peptides obtained by cyanogen bromide cleavage of its alpha-1-chain. Eur J Biochem. 1971 Apr;19(3):398–407. doi: 10.1111/j.1432-1033.1971.tb01329.x. [DOI] [PubMed] [Google Scholar]
- Tryggvason K., Risteli J., Kivirikko K. I. Separation of prolyl 3-hydroxylase and 4-hydroxylase activities and the 4-hydroxyproline requirement for synthesis of 3-hydroxyproline. Biochem Biophys Res Commun. 1976 May 23;76(2):275–281. doi: 10.1016/0006-291x(77)90722-7. [DOI] [PubMed] [Google Scholar]
- Wendt P., von der Mark K., Rexrodt F., Kühn K. The covalent structure of collagen. The amino-acid sequence of the 112-residues. Amino-terminal part of peptide 1-CB6 from calf-skin collagen. Eur J Biochem. 1972 Oct 17;30(1):169–183. doi: 10.1111/j.1432-1033.1972.tb02084.x. [DOI] [PubMed] [Google Scholar]
