Biologically Active Polypeptides ofAnemonia sulcata—and of Other Sea Anemones—Tools in the Study of Exitable Membranes

2004 ◽  
Vol 23 (4) ◽  
pp. 451-466 ◽  
Author(s):  
László Béress
Author(s):  
Vladimir M. Mahnir ◽  
Uriy N. Shumilov ◽  
Alla M. Kovalevskaya ◽  
Liudmila A. Romanenko ◽  
Sergey D. Grebelny

2013 ◽  
Vol 39 (5) ◽  
pp. 311-320
Author(s):  
V. M. Tabakmakher ◽  
M. M. Monastyrnaya ◽  
E. V. Leichenko ◽  
I. N. Gladkikh ◽  
E. A. Zelepuga ◽  
...  

2019 ◽  
Vol 3 (2) ◽  
pp. 117-136
Author(s):  
Kalina R.S. Monastyrnaya M.M.

Sea anemones are well-spread everywhere in the World Ocean and represent the most ancient active poisonous organisms. Their main instrument of attack on other animals are the nematocysts – stinging organelles with the curtailed hollow thread with poisonous edge on the end. In order to attract their potential victims, they use fluorescent proteins. These proteins became a separate object of research as genetically coded markers for the observation of activity of promotors of genes. The poisonous secret of sea anemones is characterized by the presence of maximum number of peptides of various structural classes and spatial structures among the studied land and marine organisms (bees, spiders, scorpions, snakes ect.). This fact complicates the identification of sea anemones' secret and its differentiation from poisons of animals of other taxons, if the concrete source of its origin is unknown. The toxicity of some biologically active sea anemone peptides (RpI, RpIII) at intravenous administration to experimental animals is comparable with that of the most well-known and dangerous representatives of natural toxins with the similar mechanism of action (an alpha-hemolysine and tetrodotoxin), or chemical warfare agents, such as sarin and hydrogen cyanide. Based on their toxic effect, the biologically active sea anemone peptides generally can be classified as neurotoxins due to their impact on the functioning of sodium channels in the cells of the nervous system of animals. cardiotoxic effect of sea anemone secret is caused by the specificity of interaction between its separate neurotoxins and one of the sub-types of sodium channels of muscle cells, characteristic for heart tissues. The main ways of identification of sea anemone neurotoxins in samples (for example, during the investigation of biological crimes) can be sequence by Edman`s method or tandem mass spectrometry (the analysis of fragments of toxin molecule for the establishment of its structure). Further study on the mechanisms of interaction between the sea anemone neurotoxins and the ion channels of the cells of nervous and muscular systems may result in the creation of medicines for treatment of channelopathy, as well as pluripotential antidotes, blocking the toxins, that influence on sodium channels


Peptides ◽  
1992 ◽  
Vol 13 (5) ◽  
pp. 851-857 ◽  
Author(s):  
Klaus Carstensen ◽  
Kenneth L. Rinehart ◽  
Ian D. McFarlane ◽  
Cornelis J.P. Grimmelikhuijzen

Peptides ◽  
1993 ◽  
Vol 14 (2) ◽  
pp. 131-135 ◽  
Author(s):  
Klaus Carstensen ◽  
Ian D. McFarlane ◽  
Kenneth L. Rinehart ◽  
Diane Hudman ◽  
Furong Sun ◽  
...  

Peptides ◽  
1991 ◽  
Vol 12 (6) ◽  
pp. 1165-1173 ◽  
Author(s):  
Hans-Peter Nothacker ◽  
Kenneth L. Rinehart ◽  
Ian D. McFarlane ◽  
Cornelis J.P. Grimmelikhuijzen

Toxicon ◽  
1983 ◽  
Vol 21 ◽  
pp. 289-290 ◽  
Author(s):  
D. Mebs ◽  
M. Liebrich ◽  
A. Reul

Author(s):  
Kathleen M. Marr ◽  
Mary K. Lyon

Photosystem II (PSII) is different from all other reaction centers in that it splits water to evolve oxygen and hydrogen ions. This unique ability to evolve oxygen is partly due to three oxygen evolving polypeptides (OEPs) associated with the PSII complex. Freeze etching on grana derived insideout membranes revealed that the OEPs contribute to the observed tetrameric nature of the PSIl particle; when the OEPs are removed, a distinct dimer emerges. Thus, the surface of the PSII complex changes dramatically upon removal of these polypeptides. The atomic force microscope (AFM) is ideal for examining surface topography. The instrument provides a topographical view of individual PSII complexes, giving relatively high resolution three-dimensional information without image averaging techniques. In addition, the use of a fluid cell allows a biologically active sample to be maintained under fully hydrated and physiologically buffered conditions. The OEPs associated with PSII may be sequentially removed, thereby changing the surface of the complex by one polypeptide at a time.


Author(s):  
M. Boublik ◽  
W. Hellmann ◽  
F. Jenkins

Correlations between structure and function of biological macromolecules have been studied intensively for many years, mostly by indirect methods. High resolution electron microscopy is a unique tool which can provide such information directly by comparing the conformation of biopolymers in their biologically active and inactive state. We have correlated the structure and function of ribosomes, ribonucleoprotein particles which are the site of protein biosynthesis. 70S E. coli ribosomes, used in this experiment, are composed of two subunits - large (50S) and small (30S). The large subunit consists of 34 proteins and two different ribonucleic acid molecules. The small subunit contains 21 proteins and one RNA molecule. All proteins (with the exception of L7 and L12) are present in one copy per ribosome.This study deals with the changes in the fine structure of E. coli ribosomes depleted of proteins L7 and L12. These proteins are unique in many aspects.


1959 ◽  
Vol 37 (4) ◽  
pp. 439-444 ◽  
Author(s):  
Ranwel Caputto ◽  
William O. Smith ◽  
Jordan Tang ◽  
Raul E. Trucco ◽  
Walter Joel ◽  
...  

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