B W Lubit

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We used an antibody prepared against Aplysia (mollusc) body-wall actin that specifically reacts with certain forms of cytoplasmic actin in mammalian cells to probe for the presence of actin at the neuromuscular junction. Immunocytochemical studies showed that actin or an actinlike molecule is concentrated at neuromuscular junctions of normal and denervated(More)
We elicited antibodies in rabbits to actin purified from body wall muscle of the marine mollusc, Aplysia californica. We found that this antiactin has an unusual specificity: in addition to reacting with the immunogen, it recognizes cytoplasmic vertebrate actins but not myofibrillar actin. Radioimmunoassay showed little or no cross-reaction with actin(More)
Human metaphase chromosomes, fixed in methanol-acetic acid, were ultraviolet irradiated to produce single-stranded regions of chromosomal DNA and treated with anti-5-methylcytidine. Using an immunoperoxidase procedure, regions of antibody binding were readily visualized by light microscopy in the centromeric heterochromatin regions of chromosomes 1, 9, 16,(More)
Although actin is thought to participate in several types of cell motility other than muscle contraction, no direct evidence has linked it to the force-generating mechanism for fast axonal transport. We have obtained evidence for the involvement of actin by microinjecting, into the serotonergic giant cerebral neuron of Aplysia, two preparations that have(More)
  • B W Lubit
  • 1984
Previous immunocytochemical studies in which an antibody specific for mammalian cytoplasmic actin was used showed that a high concentration of cytoplasmic actin exists at neuromuscular junctions of rat muscle fibers such that the distribution of actin corresponded exactly to that of the acetylcholine receptors. Although clusters of acetylcholine receptors(More)
Uremia has been implicated in cataractogenesis due to protein carbamylation by cyanate derived from urea. The present study was designed to directly identify the effects of carbamylation on actin polymerization and the possible contribution to cataract formation. The susceptibility of actin to carbamylation is expected because of the 19 lysines distributed(More)
A calcium binding protein (CaBP) with an apparent relative molecular weight of 28,000 was localized in the kidney of Anolis carolinensis with antisera directed against vitamin D-dependent CaBP from either rat kidney (RRCaBP) or chick intestine (CICaBP). When extracts of female saurian kidneys were fractionated by gel filtration on Sephadex G-100, both(More)
This study has focused on the characteristics of the Na+-K+-ATPase in in vitro preparations of vascular smooth muscle cells (VSMCs) derived from the rat carotid artery. The maximum velocity of enzyme reaction (Vmax) for the specific activity of the enzyme in the VSMCs' preparations was 2.36 +/- 0.04 (SE) mumol Pi X mg cell protein-1 X h-1 or 0.82 +/- 0.02(More)
The mouse monoclonal antibodies, prepared with rat beta H-crystallin as parent antigen, show cross-reactivity to specific subunits in beta H-, beta L1-, and beta L2-crystallin but no reactivity to either alpha- or gamma-crystallins. Antigenic homology among the beta-crystallin subunits was demonstrated by comparison of the topographic distributions of(More)