Variations in the Sensitivity to X-Ray-Induced Mitotic Delay during the Cell Division Cycle of the Sea Urchin Egg

1970 ◽  
Vol 42 (3) ◽  
pp. 498 ◽  
Author(s):  
Ronald C. Rustad
Keyword(s):  
Cell Division ◽  
Sea Urchin ◽  
Cell Division Cycle ◽  
X Ray ◽  
Sea Urchin Egg ◽  
Mitotic Delay

The glutathione thiol-disulfide status in the sea urchin egg during fertilization and the first cell division cycle

1976 ◽  
Vol 437 (2) ◽  
pp. 445-453 ◽  
Author(s):  
Robert C. Fahey ◽  
Stephen D. Mikolajczyk ◽  
G.Patrick Meier ◽  
David Epel ◽  
Edward J. Carroll
Keyword(s):  
Cell Division ◽  
Sea Urchin ◽  
Cell Division Cycle ◽  
Sea Urchin Egg

scholarly journals A Quantitative Description of Protoplasmic Movement During Cleavage in the Sea-Urchin Egg

1958 ◽  
Vol 35 (2) ◽  
pp. 407-424
Author(s):  
Y. HIRAMOTO
Keyword(s):  
Cell Division ◽  
Sea Urchin ◽  
Quantitative Description ◽  
Motive Force ◽  
Mitotic Apparatus ◽  
Band Theory ◽  
Cytoplasmic Granules ◽  
Carbon Particles ◽  
Sea Urchin Egg ◽  
Protoplasmic Movement

1. Protoplasmic movements during cleavage in the eggs of the heart-urchin Clypeaster japonicus have been followed by tracing the movements of cytoplasmic granules and of carbon particles adhering to the surface. 2. These movements are quantitatively described in normal eggs and in eggs whose mitotic apparatus has been destroyed by colchicine. 3. The results obtained are qualitatively similar to those obtained by Spek and by Dan and his collaborators. 4. Endoplasmic movement and changes in the length and shape of the astral rays are readily explained by the contracting-ring (band) theory. 5. The location of the motive force of cell division is discussed.

scholarly journals STUDIES ON SULFHYDRYL GROUPS DURING CELL DIVISION OF SEA URCHIN EGG

1960 ◽  
Vol 8 (3) ◽  
pp. 603-607 ◽  
Author(s):  
Hikoichi Sakai
Keyword(s):  
Cell Division ◽  
Sea Urchin ◽  
Sulfhydryl Groups ◽  
Cell Stage ◽  
Sea Urchin Eggs ◽  
Maximum Value ◽  
Sea Urchin Egg ◽  
Egg Cortex

Masses of cortices of both unfertilized and fertilized sea urchin eggs can be isolated by crushing eggs in hypotonic MaCl2 (0.1 M) solution. The amount of cortical material in terms of protein-N increases steadily after fertilization until the monaster stage and thereafter remains almost constant until well into the two-cell stage. The amount of bound—SH per protein-N of the egg cortex also increases after fertilization, reaches a maximum value at the amphiaster stage and thereafter decreases rapidly as the cleavage of the cell proceeds.

Isolation of a sea urchin egg kinesin-related protein using peptide antibodies

1992 ◽  
Vol 101 (2) ◽  
pp. 291-301 ◽  
Author(s):  
D.G. Cole ◽  
W.Z. Cande ◽  
R.J. Baskin ◽  
D.A. Skoufias ◽  
C.J. Hogan ◽  
...  
Keyword(s):  
Cell Division ◽  
Molecular Mass ◽  
Sea Urchin ◽  
Heavy Chain ◽  
Relative Molecular Mass ◽  
Related Protein ◽  
Sea Urchin Egg ◽  
Conventional Kinesin ◽  
Kinesin Superfamily ◽  
Peptide Antibodies

To understand the roles of kinesin and its relatives in cell division, it is necessary to identify and characterize multiple members of the kinesin superfamily from mitotic cells. To this end we have raised antisera to peptides corresponding to highly conserved regions of the motor domains of several known members of the kinesin superfamily. These peptide antibodies react specifically with the motor domains of kinesin and ncd protein, as expected, and they also react with several polypeptides (including kinesin heavy chain) that cosediment with microtubules (MTs) precipitated from AMPPNP-treated sea urchin egg cytosol. Subsequent fractionation of ATP eluates of these MTs yields a protein of relative molecular mass 330 × 10(3) that behaves as a complex of three polypeptides that are distinct from conventional kinesin subunits or fragments thereof. This complex contains 85 kDa and 95 kDa polypeptides, which react with our peptide antibodies, and a 115 kDa polypeptide, which does not. This triplet of polypeptides, which we refer to as KRP(85/95), binds to purified sea urchin egg tubulin in an AMPPNP-enhanced, ATP-sensitive manner and induces the formation of microtubule bundles. We therefore propose that the triplet corresponds to a novel sea urchin egg kinesin-related protein.

scholarly journals THE EFFECT OF PENICILLIN ON EGGS OF THE SEA URCHIN, ARBACIA PUNCTULATA

1945 ◽  
Vol 28 (5) ◽  
pp. 405-413 ◽  
Author(s):  
Richard J. Henry ◽  
Maryon D. Henry
Keyword(s):  
Oxygen Consumption ◽  
Cell Division ◽  
Sea Urchin ◽  
Inhibitory Action ◽  
Initial Concentration ◽  
Arbacia Punctulata ◽  
Sea Urchin Egg

1. Penicillin in the range of concentration from 250 U/ml. to approximately 2650 U/ml. inhibits the rate of cell division of the fertilized sea urchin egg from 0 to 100 per cent. 2. Penicillin in the same range of concentrations has no effect on the oxygen consumption of the unfertilized or the fertilized eggs. 3. Penicillin is bound by some component of the sea urchin egg in amounts sufficiently large to lower the initial concentration, this binding apparently not being related to the inhibitory action.

scholarly journals Studies on Sulfhydryl Groups during Cell Division of Sea Urchin Egg

1962 ◽  
Vol 45 (3) ◽  
pp. 427-438 ◽  
Author(s):  
Hikoichi Sakai
Keyword(s):  
Cell Division ◽  
Sea Urchin ◽  
Soluble Fraction ◽  
Water Soluble ◽  
The Other ◽  
Original Sample ◽  
Water Soluble Fraction ◽  
Sea Urchin Egg ◽  
Soluble Fractions

The contractility of the thread model prepared from the KCl-soluble proteins of the egg and in vivo factors for the contraction are investigated in Hemicentrotus, Anthocidaris, and Pseudocentrotus eggs. The contractility of the thread model induced by metal ions or cystine changes during development in the characteristic pattern of high at the metaphase and low at the monaster and the interkinetic stages. The change in contractility is paralleled by the change in the —SH content of the protein. The water-soluble fraction of the eggs has activity in causing contraction of the thread model. This activity changes during development in the same way as the contractility itself. The contraction of the thread induced by the water-soluble fractions is accompanied by a decrease in the —SH content of the thread. The activity of the water-soluble fraction in inducing the contraction is proportional to its ability to decrease the number of —SH groups. On boiling, the activity is largely destroyed. The activity is due to two components, one being non-dialyzable and the other dialyzable. Separately each component has little effect, but when mixed, the activity of the original sample is completely restored.

Sign in / Sign up

Export Citation Format

Share Document