Immunolocalization of the C-terminal and N-terminal regions of alpha-A and alpha-B crystallins.
The C-terminal and possibly the N-terminal regions of the alpha crystallins are thought to be involved in the molecular chaperone properties of the protein. To localize these regions within the 13-15 nm aggregate of native alpha crystallin, antisera specific for the C-terminal and N-terminal regions were used together with immunogold and transmission electron microscopy. The results demonstrate that the C-terminal regions of the alpha-A and alpha-B molecules and the N-terminal regions of the alpha-A and/or alpha-B molecules are localized to a central region of the native alpha aggregate. These findings demonstrate that the C-terminal and N-terminal regions of alpha crystallin are localized to a region of the alpha aggregate that has previously been hypothesized to be the binding site for partially denatured proteins.
Boyle
D
D
Division of Biology, Kansas State University, Manhattan 66506.
Takemoto
L
L
D000818:Animals; D000831:Animals, Newborn; D002417:Cattle; D003459:Crystallins / Q000032:analysis* / Q000302:isolation & purification; D007150:Immunohistochemistry; D007908:Lens, Crystalline / Q000737:chemistry* / Q000648:ultrastructure; D016253:Microscopy, Immunoelectron; D018832:Molecular Chaperones / Q000737:chemistry
D003459:Crystallins; D018832:Molecular Chaperones