Study on structure, anticoagulant and fibrinolytic activities of different molecular weights of heparin from clam Coelomactra antiquata

  • CHEN Guanlan ,
  • CHEN Jing ,
  • CHEN Jianping ,
  • LI Rui ,
  • JIA Xuejing ,
  • LIU Xiaofei ,
  • SONG Bingbing ,
  • ZHONG Saiyi
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  • 1(College of Food Science and Technology,Guangdong Ocean University,Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety,Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Provincial Engineering Technology Research Center of Seafood,Zhanjiang 524088,China)
    2(Collaborative Innovation Center of Seafood Deep Processing,Dalian Polytechnic University,Dalian 116034,China)

Received date: 2021-03-26

  Revised date: 2021-04-12

  Online published: 2021-09-27

Abstract

To investigate the structural properties, anticoagulant and fibrinolytic activities of different molecular weights of heparin from clam Coelomactra antiquata, heparin G2 and its two different degradation products, DG1 and DG2, were taken as the research objects in this paper. Their molecular weights were determined by high-performance gel chromatography. Fourier transform infrared spectrometer, circular dichroism spectrum, atomic force microscopy and scanning electron microscopy were used to analyze their structures. Their anticoagulant and fibrinolytic activities were evaluated by extracorporeal anticoagulant assay and fibrinolytic plate assay. The results showed that the average molecular weights of heparin G2, DG1 and DG2 were 60.25 k, 24.48 k and 6.75 kDa, respectively. The functional group structure of clam heparin did not change significantly before and after degradation, but the functional group or characteristic peak value increased with the decrease of molecular weight. While the peak value of circular dichroism spectrum of clam heparin decreased. The results of scanning electron microscope showed that the fragmented structure and spherical structure of heparin increased. And atomic force microscope showed that the reticulum linear structure of heparin was degraded into chain structure first, and then aggregated into granular structure. The anticoagulant activity of DG2 was similar to that of G2, but the anticoagulant activity of DG2 was significantly decreased. With the decrease of molecular weight, the fibrinolytic activity increased.

Cite this article

CHEN Guanlan , CHEN Jing , CHEN Jianping , LI Rui , JIA Xuejing , LIU Xiaofei , SONG Bingbing , ZHONG Saiyi . Study on structure, anticoagulant and fibrinolytic activities of different molecular weights of heparin from clam Coelomactra antiquata[J]. Food and Fermentation Industries, 2021 , 47(17) : 119 -125 . DOI: 10.13995/j.cnki.11-1802/ts.027461

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