African Journal of
Biotechnology

  • Abbreviation: Afr. J. Biotechnol.
  • Language: English
  • ISSN: 1684-5315
  • DOI: 10.5897/AJB
  • Start Year: 2002
  • Published Articles: 12488

Full Length Research Paper

Molecular cloning of full-length coding sequences and characterization of α chains for donkey (Equus asinus) type I collagen

J. Lian1,2, Y. Qin2, J. You2 and Y. Zhang1*
1State Key Laboratory of Bioreactor Engineering, East China, University of Science and Technology, Shanghai 200237, China. 2Shandong Dongeejiao Group, Shandong 252201, China.
Email: [email protected]

  •  Accepted: 05 January 2011
  •  Published: 31 July 2013

Abstract

Donkey (Equus asinus) is a good donor for the collagen production. However, the information on mRNA and protein of donkey collagen has never been reported. In this work, the cDNA sequences coding proα1 and proα2 chains of donkey type I procollagen were determined from six and seven overlapping RT-PCR products, respectively. Further characterization of deduced amino acid sequences detailed the propeptides, telopeptides and triple-helical regions in donkey type I procollagen and collagen chains. Two proα chains of donkey type I procollagen share high similarities with corresponding sequences in mammalian species observed in this study. Considering the significance of lysine and proline in the structure and function of collagen, the distribution patterns of these two characteristic residues in α chains of donkey type I collagen were observed. The mRNA expression levels of type I collagen in donkey tissues were evaluated by quantitative real-time PCR.

Key words: Collagen, Col1a1, Col1a2, donkey, complementary DNA.

Abbreviation

CDS, Coding sequences; PCR, polymerase chain reaction; qRT-PCR, quantitative real-time PCR; cDNA, complementary DNA.