Acta Veterinaria et Zootechnica Sinica ›› 2021, Vol. 52 ›› Issue (2): 498-505.doi: 10.11843/j.issn.0366-6964.2021.02.022

• BASIC VETERINARY MEDICINE • Previous Articles     Next Articles

Preparation of Bovine Surfactant Protein A and Its Antibacterial Activities

LI Nan, ZHANG Jianlou, ZHANG Yonghong, ZHENG Zhiqiang, HUO Shanshan, ZHONG Fei*, ZHAI Xianghe*   

  1. College of Animal Science and Technology/College of Veterinary Medicine, Agricultural University of Hebei, Hebei Veterinary Biotechnology Innovation Center, Hebei Technology Innovation Center of Cattle and Sheep Embryo, Baoding 071001, China
  • Received:2020-07-31 Online:2021-02-23 Published:2021-02-24

Abstract: To isolate natural bovine lung surfactant protein A (SP-A) and analyze its antibacterial activities, the maltose-sepharose (MS) beads specifically binding bovine SP-A was prepared by the covalently crosslinking method. The MS beads were used to absorb the bovine SP-A from bovine lung lavage. SDS-PAGE and Western blot detections showed that two forms of SP-A, 30 ku monomer and 60 ku dimer, were detected in the bovine SP-A preparation. The SP-A was identified as possessing the ability to aggregate E. coli, suggesting it possesses biological activity. The antibacterial experiment showed that SP-A significantly inhibited the growth of Staphylococcus aureus, Streptococcus agalactiae and the pathogenic E. coli, especially for Gram-negative bacteria with high inhibition activity, indicating that the bovine SP-A prepared in this study possesses antibacterial activities. This study provided necessary conditions for further investigation on SP-A biological characteristics and antibacterial activities, as well as opened up a new way for the development of SP-A antibacterial reagent.

Key words: bovine surfactant protein A, isolation and purification, meltose-sepharose beads, antibacterial activity

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