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2016 , Vol. 16 >Issue 4: 654 - 659

DOI: https://doi.org/10.12034/j.issn.1009-606X.216139

Biochemical Engineering

Separation and Characterization of Type II Collagen from Bovine Articular Cartilage

  • LI Sai-na KANG Ji-yao DENG Ping-ye GAO Jian-ping ZHANG Gui-feng WANG Ming-lin
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  • 1. College of Food Science and Engineering, Shandong Agricultural University
    2. Beijing Center for Physical and Chemical Analysis
    3. State Key laboratory of Biochemical Engineering, Institute of Process Engineering, CAS

Received date: 2016-02-17

  Revised date: 2016-03-23

  Online published: 2016-10-10

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Abstract

The bovine articular cartilage was pretreated using NaCl and guanidine hydrochloride to remove impurities and the proteoglycan respectively. Then the miscellaneous proteins were digested by pepsin, and the type II collagen was purified by salting out, dialysis and freeze-dried, Type II collagen was characterized. The results showed that a single band (α-chain) with a subunit molecular weight of 130 kDa. The content of Gly in amino acid composition of type II collagen was over 30%, and the total content of Pro and Hyp was over 20%. The purified type II collagen had unique supramolecular structures of collagen. The denaturation temperature of type II collagen was 43.68℃ in buffer solution with pH 7.0. Properties of collagen purified from bovine cartilage corresponded to bovine type II collagen.

Key words： collagen type II; separation; mass spectrometry; marker peptides

Cite this article

LI Sai-na KANG Ji-yao DENG Ping-ye GAO Jian-ping ZHANG Gui-feng WANG Ming-lin . Separation and Characterization of Type II Collagen from Bovine Articular Cartilage[J]. The Chinese Journal of Process Engineering, 2016 , 16(4) : 654 -659 . DOI: 10.12034/j.issn.1009-606X.216139

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