Literature DB >> 2226849

The primary structure of a triple-helical domain of collagen type VIII from bovine Descemet's membrane.

K Mann1, R Jander, E Korsching, K Kühn, J Rauterberg.   

Abstract

We have isolated and sequenced a fragment of 469 amino acid residues from bovine type VIII collagen. The sequence was composed of a series of Gly-X-Y repeats which was interrupted 8 times by short imperfections. The number and relative location of these interruptions were similar to those of chicken alpha 1(X) and rabbit alpha 1(VIII) chain triple-helical domains. Comparison to published N-terminal sequences to two triple-helical fragments of bovine type VIII collagen and to the cDNA derived sequence of the rabbit alpha 1(VIII) chain showed that this fragment was the triple-helical domain of a second type VIII collagen chain which we designate alpha 2(VIII).

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Year:  1990        PMID: 2226849     DOI: 10.1016/0014-5793(90)81076-z

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

1.  Type VIII collagen is a product of vascular smooth-muscle cells in development and disease.

Authors:  J R MacBeath; C M Kielty; C A Shuttleworth
Journal:  Biochem J       Date:  1996-11-01       Impact factor: 3.857

2.  Beta-sheet secondary structure of the trimeric globular domain of C1q of complement and collagen types VIII and X by Fourier-transform infrared spectroscopy and averaged structure predictions.

Authors:  K F Smith; P I Haris; D Chapman; K B Reid; S J Perkins
Journal:  Biochem J       Date:  1994-07-01       Impact factor: 3.857

  2 in total

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