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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.
Brazel, D; Oberbäumer, I; Dieringer, H; Babel, W; Glanville, R W; Deutzmann, R; Kühn, K.
Afiliación
  • Brazel D; Max-Planck-Institut für Biochemie, Martinsried bei München, Federal Republic of Germany.
Eur J Biochem ; 168(3): 529-36, 1987 Nov 02.
Article en En | MEDLINE | ID: mdl-3311751
ABSTRACT
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.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Membrana Basal / Colágeno Límite: Humans Idioma: En Revista: Eur J Biochem Año: 1987 Tipo del documento: Article
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Membrana Basal / Colágeno Límite: Humans Idioma: En Revista: Eur J Biochem Año: 1987 Tipo del documento: Article