A Preliminary Study on Bellamy purificata Lectin
DOI:
Author:
Affiliation:

Clc Number:

Fund Project:

  • Article
  • |
  • Figures
  • |
  • Metrics
  • |
  • Reference
  • |
  • Related
  • |
  • Cited by
  • |
  • Materials
  • |
  • Comments
    Abstract:

    By Sepharose 4B-thyroglobulin affinity column chromatography a lectin was purified from Bellamya purificata. It showed a single band on alkaline PAGE. This lectin (BPL) agglutinated red blood cells of rabbit,duck and pig,but not of human blood types or formalin and/or glutaraldehyde-fixed rabbit erythrocytes. Its agglutination activity could be inhibited by 1.0mol/L lactose or galactose as well as 60g/L thyroglobulin, but not by alkaline borate buffer.BPL was temperature-sensitive,while showed a broad optical pH range (pH4.56-9.96).

    Reference
    Related
    Cited by
Get Citation

Zhang Jiqiang, Li Qingyi. A Preliminary Study on Bellamy purificata Lectin[J]. Progress in Biochemistry and Biophysics,1995,22(3):281-283

Copy
Share
Article Metrics
  • Abstract:
  • PDF:
  • HTML:
  • Cited by:
History
  • Received:April 25,1994
  • Revised:July 16,1994
  • Accepted:
  • Online:
  • Published: