Cytoplasmic tubulin from the unfertilized sea urchin egg: II. Variation of the intrinsic calcium sensitivity of strongylocentrotus purpuratus egg tubulin as a function of temperature and brain microtubule-associated proteins

Cell Motility ◽  
1984 ◽  
Vol 4 (5) ◽  
pp. 333-350 ◽  
Author(s):  
Kathy A. Suprenant ◽  
Lionel I. Rebhun
Keyword(s):  
Sea Urchin ◽  
Strongylocentrotus Purpuratus ◽  
Calcium Sensitivity ◽  
Microtubule Associated Proteins ◽  
Sea Urchin Egg ◽  
Associated Proteins

scholarly journals Temperature and pH govern the self-assembly of microtubules from unfertilized sea-urchin egg extracts

1987 ◽  
Vol 87 (1) ◽  
pp. 71-84 ◽  
Author(s):  
K.A. Suprenant ◽  
J.C. Marsh
Keyword(s):  
Sea Urchin ◽  
Self Assembly ◽  
Ionic Composition ◽  
New Method ◽  
Temperature Dependent ◽  
Microtubule Associated Proteins ◽  
Sea Urchin Egg ◽  
The Pacific ◽  
Egg Extracts ◽  
Associated Proteins

A new method for microtubule purification from unfertilized sea-urchin eggs was developed in order to obtain large quantities of calcium- and cold-labile microtubules that contained microtubule-associated components important for mitosis. By taking into consideration the pH, ionic composition of egg cytoplasm, and the physiological temperature for growth of the Pacific coast sea-urchin Strongylocentrotus purpuratus, methods were developed for the assembly of intact microtubules directly from unfertilized egg extracts. The microtubules obtained by cycles of temperature-dependent assembly and disassembly are composed of tubulin and abundant microtubule-associated proteins. These microtubules are cold- and calcium-labile and assemble at a critical protein concentration of 0.11 mg ml-1 at 24 degrees C. The yield of microtubule protein obtained by this new method is equivalent to that obtained with taxol (6–8 mg/20 ml packed eggs). Microtubules that have been fixed and prepared for electron microscopy are decorated with large, globular projections that are attached to the microtubule by thin stalks.

The Respiratory and Glycolytic Enzymes of Sea-Urchin Eggs

1954 ◽  
Vol 31 (2) ◽  
pp. 208-217
Author(s):  
MARTYNAS YČAS
Keyword(s):  
Cytochrome C ◽  
Sea Urchin ◽  
Strongylocentrotus Purpuratus ◽  
Lactic Dehydrogenase ◽  
Glycolytic Pathway ◽  
Endogenous Respiration ◽  
Centrifugal Field ◽  
Lytechinus Pictus ◽  
Sea Urchin Eggs ◽  
Sea Urchin Egg

1. Activity corresponding to phosphoglucomutase, phosphohexoisomerase, aldolase, triosephosphate dehydrogenase, enolase and lactic dehydrogenase has been demonstrated in homogenates prepared from unfertilized sea-urchin eggs (Strongylocentrotus purpuratus and Lytechinus pictus). 2. The presence of cytochromes a and b1 has been confirmed. These cytochromes sediment in a relatively low centrifugal field. 3. No cytochrome c could be demonstrated, although cytochrome c is both reduced and oxidized by homogenates, and addition of cytochrome c increases the endogenous respiration and oxidation of succinate. 4. These results support the view that the usual glycolytic pathway operates in the sea-urchin egg and is the principal route of oxidation of carbohydrate.

Isolation of Mitotic Microtubule-Associated Proteins from Sea Urchin Eggs

1986 ◽  
Vol 466 (1 Dynamic Aspec) ◽  
pp. 328-339 ◽  
Author(s):  
GEORGE S. BLOOM ◽  
FRANCIS C. LUCA ◽  
CHRISTINE A. COLLINS ◽  
RICHARD B. VALLEE
Keyword(s):  
Sea Urchin ◽  
Microtubule Associated Proteins ◽  
Sea Urchin Eggs ◽  
Associated Proteins

scholarly journals Hierarchies of protein cross-linking in the extracellular matrix: involvement of an egg surface transglutaminase in early stages of fertilization envelope assembly.

1988 ◽  
Vol 107 (6) ◽  
pp. 2447-2454 ◽  
Author(s):  
D E Battaglia ◽  
B M Shapiro
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Physiological Function ◽  
Strongylocentrotus Purpuratus ◽  
Cross Linking ◽  
Early Step ◽  
Transglutaminase Activity ◽  
Sea Urchin Egg ◽  
A Cell ◽  
Secretory Products

The involvement of transglutaminase activity in fertilization envelope (FE) formation was investigated using eggs from the sea urchin, Strongylocentrotus purpuratus. Eggs fertilized in the presence of the transglutaminase inhibitors, putrescine and cadaverine, had disorganized and expanded FEs with inhibition of the characteristic I-T transition. The permeability of the FE was increased by these agents, as revealed by the loss of proteins from the perivitelline space and the appearance of ovoperoxidase activity in supernates from putrescine-treated eggs. [3H]putrescine was incorporated into the FE during fertilization in a reaction catalyzed by an egg surface transglutaminase that could also use dimethylcasein as a substrate in vitelline layer-denuded eggs. Egg secretory products alone had no transglutaminase activity. The cell surface transglutaminase activity was transient and maximal within 4 min of activation. The enzyme was Ca2+ dependent and was inhibited by Zn2+. We conclude that sea urchin egg surface transglutaminase catalyzes an early step in a hierarchy of cross-linking events during FE assembly, one that occurs before ovoperoxidase-mediated dityrosine formation (Foerder, C. A., and B. M. Shapiro. 1977. Proc. Natl. Acad. Sci. USA. 74:4214-4218). Thus it provides a graphic example of the physiological function of a cell surface transglutaminase.

scholarly journals Colchicine-binding activity distinguishes sea urchin egg and outer doublet tubulins.

1984 ◽  
Vol 99 (1) ◽  
pp. 37-41 ◽  
Author(s):  
L Wilson ◽  
H P Miller ◽  
T A Pfeffer ◽  
K F Sullivan ◽  
H W Detrich
Keyword(s):  
Sea Urchin ◽  
Strongylocentrotus Purpuratus ◽  
Binding Activity ◽  
Binding Affinities ◽  
Regulatory Site ◽  
Colchicine Binding Site ◽  
Sea Urchin Egg ◽  
Enthalpy And Entropy Changes ◽  
Enthalpy And Entropy ◽  
Significant Chemical

The colchicine-binding activity of tubulin has been utilized to distinguish the tubulins from two distinct microtubule systems of the same species, the sea urchin Strongylocentrotus purpuratus. We have analyzed the colchicine-binding affinities of highly purified tubulins from the unfertilized eggs and from the flagellar outer doublet microtubules by van't Hoff analysis, and have found significant differences in the free energy, enthalpy, and entropy changes characterizing the binding of colchicine to the two tubulins. The data indicate that significant chemical differences in the tubulins from the two functionally distinct microtubule systems exist, and that the differences are expressed in the native forms of the tubulins. Our findings are discussed in terms of the possibility that the colchicine-binding site may be an important regulatory site on the tubulin molecule.

Phosphate-Transport Appearance in the Sea-Urchin Egg. II. Analysis of the Genome Function with Centrifuged Eggs and Ethidium Bromide

1974 ◽  
Vol 52 (6) ◽  
pp. 1186-1191
Author(s):  
Joël de la Noüe
Keyword(s):  
Ethidium Bromide ◽  
Sea Urchin ◽  
Phosphate Uptake ◽  
Strongylocentrotus Purpuratus ◽  
Nuclear Genome ◽  
Phosphate Transport ◽  
Carrier System ◽  
Purple Sea Urchin ◽  
Sea Urchin Egg ◽  
Phosphate Carrier

Ethidium bromide, an inhibitor of mitochondrial transcription, inhibits phosphate uptake, valine incorporation, and uridine incorporation in fertilized eggs of Strongylocentrotus purpuratus, the purple sea urchin. Phosphate uptake, valine incorporation, and valine influx are also inhibited by this drug in artificially activated nucleate and anucleate egg fragments. Ethidium bromide does not affect the egg respiration and it has no measurable effect on ATP level and labeling. It is concluded that the post-fertilization appearance of the phosphate-carrier system does not require the participation of the nuclear genome but that of the mitochondrial one. It is likely that the same proposal holds for the L-valine-transport system. Some effects of ethidium bromide on development are exposed.

The GTP-binding protein RhoA localizes to the cortical granules of Strongylocentrotus purpuratus sea urchin egg and is secreted during fertilization

2000 ◽  
Vol 79 (2) ◽  
pp. 81-91 ◽  
Author(s):  
Patricia Cuéllar-Mata ◽  
Guadalupe Martínez-Cadena ◽  
Juana López-Godínez ◽  
Armando Obregón ◽  
Jesús García-Soto
Keyword(s):  
Sea Urchin ◽  
Binding Protein ◽  
Strongylocentrotus Purpuratus ◽  
Cortical Granules ◽  
Gtp Binding Protein ◽  
Gtp Binding ◽  
Sea Urchin Egg
Sign in / Sign up

Export Citation Format

Share Document