The identification and properties of chitin-binding protein b01 (CBPb01). Academic Article

abstract

• Bovine serum contains N-acetyl-D-glucosamine (GlcNAc)-sensitive opsonin inhibitory factors. In the present study, a major component of chitin-binding protein (chitin-binding protein b01, CBPb01) was purified from bovine serum, and identified CBPb01 as bovine IgM by its subunit structure, antigenic properties, and partial sequences. The results of a lectin-binding assay showed that the heavy chain of CBPb01 had a GlcNAc structure, but the commercial IgM did not. It is possible that CBPb01 interconnects through its GlcNAc structure, subsequently forming complexes. We also demonstrated that CBPb01 had opsonin-inhibitory activity, and that this activity was dependent on the binding of CBPb01 to GlcNAc on the zymosan surface. These findings indicate the presence of a kind of IgM that recognizes GlcNAc structure in the regulation of opsonization.

authors

• Suzuki, Masako

published proceedings

• J Vet Med Sci

author list (cited authors)

• Suzuki, M., Morimatsu, M., & Syuto, B.

citation count

• 1

publication date

• June 2002

publisher

• Japanese Society of Veterinary Science  Publisher

keywords

• Acetylglucosamine
• Amino Acid Sequence
• Animals
• Blood Proteins
• Cattle
• Chitin
• Chromatography, Gel
• Female
• Immunodiffusion
• Immunoglobulin M
• Molecular Sequence Data
• Molecular Weight
• Opsonin Proteins
• Sequence Alignment
• Sequence Analysis, Protein
• Zymosan

PubMed Central ID

• 12130830

Digital Object Identifier (DOI)

• 10.1292/jvms.64.477

start page

• 477

end page

• 481

volume

• 64

issue

• 6

URL

• http://dx.doi.org/10.1292/jvms.64.477