scholarly journals Carotenoid distribution in the gonads of the limpets Patella vulgata and Patella depressa

1950 ◽  
Vol 47 (2) ◽  
pp. 249-251 ◽  
Author(s):  
T. W. Goodwin
Keyword(s):  
Patella Vulgata

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

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.

scholarly journals alpha-N-acetylgalactosaminidase from the limpet, Patella vulgata.

1977 ◽  
Vol 252 (15) ◽  
pp. 5194-5200 ◽  
Author(s):  
Y Uda ◽  
S C Li ◽  
Y T Li
Keyword(s):  
Patella Vulgata

The Histochemistry of the Radula of Patella vulgata

1961 ◽  
Vol s3-102 (59) ◽  
pp. 371-380
Author(s):  
N. W. RUNHAM
Keyword(s):  
Amino Groups ◽  
Patella Vulgata ◽  
Quinone Tanning ◽  
Histochemical Changes

When first secreted the radula consists of chitin and protein. In the bases and cusps of the teeth the reactions for tyrosine, tryptophane, and chitin become negative, and are replaced by reactions for amino groups and argentaffin material. The bases of the teeth become impregnated with iron. Subsequently the reactions for amino groups and argentaffin material become negative in the cusps and they then become impregnated with iron and silica. Very few changes have been observed in the radular membrane. It is suggested that the occurrence of quinone tanning might account for these histochemical changes observed in the radula, but phenols derived from tryptophane would appear to be more important in the tanning of the radula than those derived from tyrosine.

Sign in / Sign up

Export Citation Format

Share Document