Time Partitioning of Foraging in the Limpet Patella vulgata

10.2307/5298 ◽  
1991 ◽  
Vol 60 (2) ◽  
pp. 563 ◽  
Author(s):  
Matthew R. Evans ◽  
Gray A. Williams
Keyword(s):  
Patella Vulgata ◽  
Time Partitioning

Protein Synthesis Controls Cyclin Stability in Metaphase I-Arrested Oocytes of Patella vulgata

1993 ◽  
Vol 208 (2) ◽  
pp. 518-521 ◽  
Author(s):  
Pierre Colas ◽  
Catherine Launay ◽  
André E. van Loon ◽  
Pierre Guerrier
Keyword(s):  
Protein Synthesis ◽  
Patella Vulgata ◽  
Metaphase I

scholarly journals The carotenoids of the gonads of the limpets Patella vulgata and Patella depressa

1950 ◽  
Vol 47 (2) ◽  
pp. 244-249 ◽  
Author(s):  
T. W. Goodwin ◽  
M. M. Taha
Keyword(s):  
Patella Vulgata

scholarly journals Genetic recombination as a generalised gradient flow

2021 ◽  
Author(s):  
Frederic Alberti
Keyword(s):  
Arbitrary Number ◽  
Genetic Recombination ◽  
Reaction Network ◽  
Gradient Flow ◽  
Mass Action ◽  
Gradient System ◽  
Gradient Structure ◽  
Law Of Mass Action ◽  
Reversible Chemical Reaction ◽  
Time Partitioning

AbstractIt is well known that the classical recombination equation for two parent individuals is equivalent to the law of mass action of a strongly reversible chemical reaction network, and can thus be reformulated as a generalised gradient system. Here, this is generalised to the case of an arbitrary number of parents. Furthermore, the gradient structure of the backward-time partitioning process is investigated.

scholarly journals Desulphation of chondroitin sulphate by an enzyme from Patella vulgata

1968 ◽  
Vol 109 (2) ◽  
pp. 14P-15P ◽  
Author(s):  
P F Lloyd ◽  
R J Fielder
Keyword(s):  
Chondroitin Sulphate ◽  
Patella Vulgata

Aerial and underwater metabolism of Patella vulgata L.: comparison of three intertidal levels

Hydrobiologia ◽  
2012 ◽  
Vol 702 (1) ◽  
pp. 241-253 ◽  
Author(s):  
Morgana Tagliarolo ◽  
Jacques Grall ◽  
Laurent Chauvaud ◽  
Jacques Clavier
Keyword(s):  
Patella Vulgata

scholarly journals Purification and properties of α-d-mannosidase from the limpet, Patella vulgata

1970 ◽  
Vol 117 (1) ◽  
pp. 129-137 ◽  
Author(s):  
Sybil M. Snaith ◽  
G. A. Levvy ◽  
A. J. Hay
Keyword(s):  
Metal Ion ◽  
Reversible Inactivation ◽  
Patella Vulgata ◽  
Full Activity ◽  
Acid Ph ◽  
Purification And Properties ◽  
Rate Of Reaction ◽  
Metal Ion Complex

1. α-Mannosidase from the limpet, Patella vulgata, was purified nearly 150-fold, with 40% recovery. β-N-Acetylglucosaminidase was removed from the preparation by treatment with ethanol. The final product was virtually free from β-galactosidase. 2. Limpet α-mannosidase was assayed at pH3.5 and at this pH it was necessary to add Zn2+ for full activity. At pH5, the enzyme had the same activity in the presence or absence of added Zn2+. 3. On incubation at acid pH, the enzyme underwent reversible inactivation, which was prevented by adding Zn2+. 4. EDTA accelerated inactivation and the addition of Zn2+ at once restored activity. No other cation was found to reactivate the enzyme. 5. Cl- had an unspecific effect on hydrolysis by limpet α-mannosidase. It increased the rate of reaction with substrate. The anion did not prevent or reverse inactivation by EDTA. 6. It is concluded that α-mannosidase is a metalloenzyme or enzyme–metal ion complex, dissociable at the pH of activity, and that it requires Zn2+ specifically.

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