Size-Related Functional and Energetic Constraints in the Foraging of the Limpet Patella vulgata (Mollusca, Gastropoda)

1995 ◽  
Vol 9 (4) ◽  
pp. 551 ◽  
Author(s):  
G. Santini ◽  
G. Chelazzi ◽  
P. Della Santina
Keyword(s):  
Patella Vulgata ◽  
Energetic Constraints

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 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

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

scholarly journals Is behavioural plasticity consistent across different environmental gradients and through time?

2017 ◽  
Vol 284 (1860) ◽  
pp. 20170893 ◽  
Author(s):  
David J. Mitchell ◽  
Peter A. Biro
Keyword(s):  
Food Deprivation ◽  
Environmental Gradients ◽  
Reaction Norm ◽  
Environmental Variable ◽  
Behavioural Plasticity ◽  
Thermally Responsive ◽  
State Dependent ◽  
Energetic Constraints ◽  
High Consistency ◽  
Outstanding Question

Despite accumulating evidence for individual variation in behavioural plasticity, there is currently little understanding of the causes and consequences of this variation. An outstanding question is whether individual reaction norm (RN) slopes are consistent across different environmental variables—that is, whether an individual that is highly responsive to one environmental variable will be equally responsive to a second variable. Another important and related question is whether RNs are themselves consistently expressed through time or whether they are simply state dependent. Here, we quantified individual activity rates of zebrafish in response to independent manipulations of temperature and food availability that were repeated in discrete ‘bursts’ of sampling through time. Individuals that were thermally responsive were not more responsive to food deprivation, but they did exhibit greater unexplained variation. Individual RN slopes were consistent (repeatable) over time for both temperature (Rslope= 0.92) and food deprivation responses (Rslope= 0.4), as were mean activity rates in the standard environment (Rintercept= 0.83). Despite the high potential lability of behaviour, we have demonstrated consistency of behavioural RN components and identified potential energetic constraints leading to high consistency of thermal RNs and low consistency of food deprivation RNs.

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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