The covalent structure of calf skin type III collagen. I. The amino acid sequence of the amino terminal region of the alpha 1(III) chain (position 1--222)
- PMID: 488906
- DOI: 10.1515/bchm2.1979.360.2.809
The covalent structure of calf skin type III collagen. I. The amino acid sequence of the amino terminal region of the alpha 1(III) chain (position 1--222)
Abstract
The amino terminal 227 amino acid residues of the alpha 1(III) chain contain four CNBr peptides: alpha 1(III)CB3A (79 residues), CB3B, CB3C (6 residues each), CB7 (37 residues) and CB6 (99 residues). Fragmentation of the CNBr peptides was carried out using trypsin, chymotrypsin and the protease from Staphylococcus aureus V8. The fragments obtained were isolated by a combination of molecular sieve and ion exchange chromatography. The sequence analysis was performed according to the automated Edman degradation procedure.
Similar articles
-
The covalent structure of calf skin type III collagen. V. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB9A (position 789 to 927).Hoppe Seylers Z Physiol Chem. 1979 Jul;360(7):851-60. Hoppe Seylers Z Physiol Chem. 1979. PMID: 488910
-
The covalent structure of calf skin type III collagen. II. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB1,8,10,2(Positions 223--402).Hoppe Seylers Z Physiol Chem. 1979 Jul;360(7):821-32. Hoppe Seylers Z Physiol Chem. 1979. PMID: 488907
-
The covalent structure of calf skin type III collagen. IV. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB5 (positions 552--788).Hoppe Seylers Z Physiol Chem. 1979 Jul;360(7):841-50. Hoppe Seylers Z Physiol Chem. 1979. PMID: 488909
-
The covalent structure of calf skin type III collagen. VI. The amino acid sequence of the carboxyterminal cyanogen bromide peptide alpha 1(III)CB9B (position 928--1028).Hoppe Seylers Z Physiol Chem. 1979 Jul;360(7):861-8. Hoppe Seylers Z Physiol Chem. 1979. PMID: 488911
-
The covalent structure of calf skin type III collagen. III. The amino acid sequence of the cyanogen bromide peptide alpha 1(III)CB4 (positions 403--551).Hoppe Seylers Z Physiol Chem. 1979 Jul;360(7):833-40. Hoppe Seylers Z Physiol Chem. 1979. PMID: 488908
Cited by
-
The major clotting protein from guinea pig seminal vesicle contains eight repeats of a 24-amino acid domain.Proc Natl Acad Sci U S A. 1987 Oct;84(19):6712-4. doi: 10.1073/pnas.84.19.6712. Proc Natl Acad Sci U S A. 1987. PMID: 3477802 Free PMC article.
-
Nucleotide sequence of a cDNA coding for the amino-terminal region of human prepro alpha 1(III) collagen.Nucleic Acids Res. 1988 Jul 25;16(14B):7201. doi: 10.1093/nar/16.14.7201. Nucleic Acids Res. 1988. PMID: 3405773 Free PMC article. No abstract available.
-
Type III collagen (COL3A1): Gene and protein structure, tissue distribution, and associated diseases.Gene. 2019 Jul 30;707:151-171. doi: 10.1016/j.gene.2019.05.003. Epub 2019 May 7. Gene. 2019. PMID: 31075413 Free PMC article. Review.
-
Structure of cDNA clones coding for the entire prepro alpha 1 (III) chain of human type III procollagen. Differences in protein structure from type I procollagen and conservation of codon preferences.Biochem J. 1989 Jun 1;260(2):509-16. doi: 10.1042/bj2600509. Biochem J. 1989. PMID: 2764886 Free PMC article.
-
Cross-link analysis of the C-telopeptide domain from type III collagen.Biochem J. 1996 Sep 1;318 ( Pt 2)(Pt 2):497-503. doi: 10.1042/bj3180497. Biochem J. 1996. PMID: 8809038 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Molecular Biology Databases