Isolation of chick tenascin variants and fragments. A C-terminal heparin-binding fragment produced by cleavage of the extra domain from the largest subunit splicing variant.

Abstract excerpt

The extracellular-matrix glycoprotein, tenascin, consists of disulfide-linked subunits of 190, 200 and 230 kDa (the three splicing variants reported in chicken) and usually exists as a six-armed structure under the electron microscope. We used monoclonal antibodies to isolate and characterize different splicing variants and proteolytic fragments obtained from the native protein. Purified monomeric tenascin has a...

Topics

• Animals
• Antibodies, Monoclonal
• Binding Sites
• Cell Adhesion
• Cell Adhesion Molecules, Neuronal
• Cells, Cultured
• Chick Embryo
• Electrophoresis, Gel, Two-Dimensional
• Extracellular Matrix Proteins
• Genetic Variation