Completion of the amino acid sequence of the alpha 1 chain of human basement membrane collagen (type IV) reveals 21 non-triplet interruptions located within the collagenous domain
Autor: | Klaus Kühn, Rainer Deutzmann, Hans Dieringer, Dieter Brazel, Robert W. Glanville, Wilfried Babel, Ilse Oberbäumer |
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Rok vydání: | 1987 |
Předmět: |
Molecular Sequence Data
Biology Biochemistry Primer extension Basement Membrane chemistry.chemical_compound Protein sequencing Complementary DNA medicine Humans Amino Acid Sequence Cysteine RNA Messenger Cloning Molecular Peptide sequence Sequence (medicine) Basement membrane Base Sequence Oligonucleotide Hydrolysis DNA Molecular biology Peptide Fragments medicine.anatomical_structure chemistry Genes Cyanogen bromide Collagen Peptide Hydrolases |
Zdroj: | European journal of biochemistry. 168(3) |
ISSN: | 0014-2956 |
Popis: | The cDNA and protein sequences of the N-terminal half of human basement membrane collagen (type IV) have been determined. Overlapping cDNA clones were constructed by repeated primer extension with synthetic oligonucleotides. They cover 2953 bp, beginning at the 5' end of the corresponding mRNA. At the protein level, the sequence of the cyanogen bromide peptide CB6 adjacent to the 7S domain has been additionally elucidated. The data presented here complete the protein sequence and nearly the entire cDNA sequence of the human alpha 1(IV) chain. The amino-terminal half of the alpha 1(IV) chain contains 8 cysteine residues involved in intramolecular and intermolecular cross-links. The entire triple-helical domain of alpha 1(IV) is interrupted by 21 non-triplet regions. |
Databáze: | OpenAIRE |
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