Isolation and characterization of a galactose-specific carbohydrate binding protein from human lymphoblastic cells

Biochem Biophys Res Commun. 1990 Dec 31;173(3):1079-85. doi: 10.1016/s0006-291x(05)80896-4.

Abstract

A carbohydrate binding protein of Mr = 32,000 (CBP 32) has been isolated from detergent extracts of human B and T lymphoblastoid cells. CBP 32 binds specifically to glycoproteins containing asparagine-linked complex oligosaccharides, and can be eluted from a fetuin affinity matrix by beta-lactose. Binding is not thiol dependent, nor are divalent cations necessary for binding. Native CBP 32 appears to exist as a monomer, with a pI of 8.2. Purified CBP 32 can bind detergent, as shown by charge-shift electrophoresis, and thus appears to be an integral membrane protein.

MeSH terms

  • B-Lymphocytes / chemistry*
  • Carrier Proteins / isolation & purification*
  • Cell Line
  • Detergents
  • Electrophoresis, Polyacrylamide Gel
  • Galactosides / metabolism
  • Galectins
  • Hemagglutinins / isolation & purification*
  • Humans
  • Isoelectric Focusing
  • Molecular Weight
  • T-Lymphocytes / chemistry*

Substances

  • Carrier Proteins
  • Detergents
  • Galactosides
  • Galectins
  • Hemagglutinins