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In three separate experiments using auditory stimuli, subjects detected improbable targets in an on-going train of standard stimuli. In experiment I there were two equally improbable target stimuli, one difficult to discriminate from the standard stimuli and one easy to discriminate. Experiment II investigated the effects of discrimination difficulty using(More)
Two proteins, with molecular weights of 49 (CP49) and 115 kDa (CP115) as judged by SDS PAGE, have been shown by immunocytochemistry to be components of the beaded filament, a cytoskeletal structure thus far demonstrated only in the lens fiber cell. We have used antibodies reactive with CP49 to screen a mouse lens cDNA expression library. An immunoreactive(More)
PURPOSE The 129 strain of mouse carries a mutation in the gene for CP49 (phakinin), an intermediate filament protein thus far demonstrated only in the lens fiber cell. As such, these mice represent naturally occurring mutants of interest in the study of the lens cytoskeleton. However, this strain of mouse is also widely used as a source of embryonic stem(More)
We have previously established the utility of site-directed spin labeling and electron paramagnetic resonance to determine structural relationships among proteins in intact intermediate filaments. Using this same approach we have introduced spin labels at 21 residues between amino acids 169 and 193 in rod domain 1 of human vimentin. The electron(More)
PURPOSE To describe a previously uncharacterized structural specialization in the mouse lens fiber cell and to delineate its emergence relative to lens development and fiber cell differentiation. METHODS Lens fixation efficiency was explored using (14)C-formaldehyde and autoradiography. Lens fiber cell architecture was examined by scanning electron(More)
The cDNA coding for calf filensin, a membrane-associated protein of the lens fiber cells, has been cloned and sequenced. The predicted 755-amino acid-long open reading frame shows primary and secondary structure similarity to intermediate filament (IF) proteins. Filensin can be divided into an NH2-terminal domain (head) of 38 amino acids, a middle domain(More)
PURPOSE To determine whether the chaperone activity of human alpha-crystallin can protect a restriction enzyme from heat inactivation. METHODS The restriction enzyme Nde I was heated in the presence or absence of purified bovine alpha-crystallin. Following heat treatment, the enzymatic activity of the heat treated samples was assayed by cleavage of(More)
Phosphorylation drives the disassembly of the vimentin intermediate filament (IF) cytoskeleton at mitosis. Chromatographic analysis has suggested that phosphorylation produces a soluble vimentin tetramer, but little has been determined about the structural changes that are caused by phosphorylation or the structure of the resulting tetramer. In this study,(More)
Site-directed spin labeling and electron paramagnetic resonance were used to probe residues 281-304 of human vimentin, a region that has been predicted to be a non-alpha-helical linker and the beginning of coiled-coil domain 2B. Though no direct test of linker structure has ever been made, this region has been hypothesized to be flexible with the(More)