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. 1987

D Brazel, and I Oberbäumer, and H Dieringer, and W Babel, and R W Glanville, and R Deutzmann, and K Kühn
Max-Planck-Institut für Biochemie, Martinsried bei München, Federal Republic of Germany.

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.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010447 Peptide Hydrolases Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES. Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, Peptide
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D003094 Collagen A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH). Avicon,Avitene,Collagen Felt,Collagen Fleece,Collagenfleece,Collastat,Dermodress,Microfibril Collagen Hemostat,Pangen,Zyderm,alpha-Collagen,Collagen Hemostat, Microfibril,alpha Collagen
D003545 Cysteine A thiol-containing non-essential amino acid that is oxidized to form CYSTINE. Cysteine Hydrochloride,Half-Cystine,L-Cysteine,Zinc Cysteinate,Half Cystine,L Cysteine
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D005796 Genes A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms. Cistron,Gene,Genetic Materials,Cistrons,Genetic Material,Material, Genetic,Materials, Genetic
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006868 Hydrolysis The process of cleaving a chemical compound by the addition of a molecule of water.

Related Publications

D Brazel, and I Oberbäumer, and H Dieringer, and W Babel, and R W Glanville, and R Deutzmann, and K Kühn
March 1985, European journal of biochemistry,
D Brazel, and I Oberbäumer, and H Dieringer, and W Babel, and R W Glanville, and R Deutzmann, and K Kühn
September 1984, European journal of biochemistry,
D Brazel, and I Oberbäumer, and H Dieringer, and W Babel, and R W Glanville, and R Deutzmann, and K Kühn
October 1985, European journal of biochemistry,
D Brazel, and I Oberbäumer, and H Dieringer, and W Babel, and R W Glanville, and R Deutzmann, and K Kühn
January 1988, FEBS letters,
D Brazel, and I Oberbäumer, and H Dieringer, and W Babel, and R W Glanville, and R Deutzmann, and K Kühn
December 1987, FEBS letters,
D Brazel, and I Oberbäumer, and H Dieringer, and W Babel, and R W Glanville, and R Deutzmann, and K Kühn
January 1990, Connective tissue research,
D Brazel, and I Oberbäumer, and H Dieringer, and W Babel, and R W Glanville, and R Deutzmann, and K Kühn
October 1983, The Biochemical journal,
D Brazel, and I Oberbäumer, and H Dieringer, and W Babel, and R W Glanville, and R Deutzmann, and K Kühn
July 1990, Biochemical and biophysical research communications,
D Brazel, and I Oberbäumer, and H Dieringer, and W Babel, and R W Glanville, and R Deutzmann, and K Kühn
May 1994, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!