Results 151 to 160 of about 25,429 (197)

Enucleation of mammalian cells with cytochalasin B

Experimental Cell Research, 1972
Abstract L cells and chinese hamster cells growing on coverslips can be enucleated by centrifugation at 3 000 g (glass coverslips) or 5 800 g (plastic coverslips) for 40 min at 35 ° to 37 °C in medium containing 10 μg/ml of cytochalasin B. The enucleated cells incorporate 3H-leucine, support replication of vaccinia virus DNA, and are viable for at ...
D M, Prescott, D, Myerson, J, Wallace
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Cytochalasin B inhibits thyroid secretion

Biochemical and Biophysical Research Communications, 1971
The addition in vitro of cytochalasin B at concentrations of 0.5–3.0 μg/ml to prelabeled mouse thyroid glands interferes with release of iodine derived from thyroglobulin and blocks colloid endocytosis. It is suggested that cytoplasmic microfilaments are involved in the secretory process.
J A, Williams, J, Wolff
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Cytochalasin B binding by human platelets

Journal of Cellular Physiology, 1982
AbstractIntact human platelets bind cytochalasin B (CB) with a capacity of 100– 120 p mols CB/mg protein or approximately 7 × 104 molecules/cell and dissociation constants (KD) ranging from 2 × 10−8 to 10−6 M. Up to 85% of this saturable binding is displaced by 10−5 M cytochalasin E (CE).
C R, Zobel, C Y, Jung
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Structure of cytochalasins and cytochalasin B binding sites in human erythrocyte membranes

Biochemistry, 1980
Twenty cytochalasins were tested for binding to and for inhibition of glucose transport in human erythrocyte membrane. In this membrane three cytochalasin B (CB) binding sites have been identified. All but three of the cytochalasins bind at site II. On the other hand, only nine of them, which are structurally closely related, bind at site I and inhibit
A L, Rampal, H B, Pinkofsky, C Y, Jung
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Binding of cytochalasin B to platelets

Journal of Cellular Biochemistry, 1989
AbstractThe binding of cytochalasin B (CB) to human platelets and to isolated platelet cytosol and membranes has been analyzed with [3H]CB. High‐ and low affinity classes of saturable binding sites were associated with intact platelets. Binding at very low concentrations of CB (i.e., high‐affinity binding) was partially prevented by 100 mM D‐galatose ...
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On the molecular basis of action of cytochalasin B

Journal of Supramolecular Structure, 1974
AbstractTritium‐labeled cytochalasin B binds rapidly and reversibly to mammalian cells, and a class of high‐affinity sites (Kn ≅ 10−7 M) and a class of low‐affinity sites (KD ⩾ 10−5 M) are detected. In red blood cells, the high‐affinity binding sites (about 3 × 105 per cell) are associated with the plasma membrane, and at least 80% of these appear to ...
S, Lin, J A, Spudich
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General Polyploid produced by Cytochalasin B

Nature New Biology, 1973
CYTOCHALASIN B prevents cytokinesis but not mitosis, and causes cells to become binucleate1. It also reduces motility1, endocytosis, phagocytosis2 and transport3,4 and causes extrusion of the nucleus to produce enucleate cells1,5,6. It has been suggested that cytochalasin B acts by an effect on the microfilament system but this remains controversial ...
V, Defendi, M G, Stoker
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Induction of triploidy in the mouse by cytochalasin B

Development, 1975
ABSTRACT Mouse eggs fertilized in vivo were treated with cytochalasin B in vitro (5 µg/ml of culture medium) at the moment of extrusion of the second polar body (2·5, 3·0, 3·5 h after copulation). Cytochalasin B inhibits cytokinesis of the second maturation division, so that triploid digynic eggs are formed in over 50% of treated eggs.
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Coelomocyte cytoskeletons Interaction with cytochalasin B

Experimental Cell Research, 1980
Abstract Cytochalasin B (CB) quickly distorts the gross morphology of sea urchin petaloid coelomocytes at low (0.1 μg/ml) concentrations and inhibits the cell's ability to morphologically transform to the filopodial form. Neither the ultrastructure nor the biochemical components of these cells are altered during these initial effects.
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Cytochalasin B and Release of Growth Hormone

Nature New Biology, 1971
MICROTUBULES are believed to be involved in emiocytosis, in which secretory granules migrate and fuse with the cell membrane, thereby liberating the granule contents into the extracellular space. Important evidence for this is that the release of insulin from pancreatic islets of Langerhans1,2, histamine from mast cells3 and from leucocytes4 and ...
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