Purification and assays of tachylectin-2

Shun ichiro Kawabata, Toshio Shibata

Research output: Chapter in Book/Report/Conference proceedingChapter


Tachylectin-2, a 27-kDa protein consisting of a five-bladed β-propeller structure, is purified by three steps of chromatography, including dextran sulfate-Sepharose CL-6B, CM-Sepharose CL-6B, and Mono S. Three isolectins of tachylectin-2 including tachylectin-2a, -2b, and -2c are purified. These isolectins exhibit hemagglutinating activity against human A-type erythrocytes in a Ca2+-independent manner with tachylectin-2b showing the highest activity. Tachylectin-2b specifically agglutinates Staphylococcus saprophyticus KD. The tachylectin-2b-mediated hemagglutination is inhibited in the presence of GlcNAc and GalNAc. The association constants for GlcNAc and GalNAc are Ka = 1.95 × 104 M−1 and Ka = 1.11 × 103 M−1, respectively. Ultracentrifugation analysis shows that tachylectin-2b is present in monomer form in solution.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages8
Publication statusPublished - 2020

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics


Dive into the research topics of 'Purification and assays of tachylectin-2'. Together they form a unique fingerprint.

Cite this