Limpets

In Mollusca, bioluminescence occurs in a great variety of organisms having distinctly different appearances, such as the classes Gastropoda (limpets, snails and sea hares), Bivalvia (clams), and Cephalopoda (squids and octopuses). All luminous molluscs currently known are marine organisms, except the New Zealand fresh water limpet Latia neritoides and the Malaysian land snail Quantula (Dyakia) striata. No information is yet available on the biochemical aspects of the Quantula luminescence. 

The New Zealand freshwater limpet Latia neritoides (Fig. 6.1.1) is the only known example of a freshwater luminous organism, with two possible exceptions certain species of luminous bacteria and the larvae of certain species of fireflies. The limpet inhabits shallow clear streams in the North Island of New Zealand, clinging to stones and rocks. Latia has a small oval-shaped shell (6-8 mm long), and secretes a luminous mucus that emits a greenish glow around the body only when disturbed the limpet does not show a spontaneous luminescence. The luminescence of Latia was first reported by Suter (1890) and further details including a positive luciferin-luciferase reaction were described by Bowden (1950). Both the luciferin and the luciferase have... 

Fig. 6.1.1 The freshwater limpet Latia neritoides in day light (left) and in the dark (right).

Bowden, B. J. (1950). Some observations on a luminescent freshwater limpet from New Zealand. Biol. Bull. 99 373-380. 

Shimomura, O., Johnson, F. H., and Haneda, Y. (1966b). Isolation of the luciferin of the New Zealand fresh-water limpet, Latia neritoides Gray. In Johnson, F. H., and Haneda, Y. (eds.), Bioluminescence in Progress, pp. 391-404. Princeton University Press, Princeton, NJ. 

The production of benzylpenicillin is very sensitive to temperature. A lot of metabolic heat is generated and the fermentation temperature has to be reduced by controlled cooling. This heat transfer is achieved by circulating chilled water through banks of pipes inside the vessel (which also serve as baffles) or through external limpet coils on the jacket of the vessel. These coils consist of continuous lengths of pipe welded in a shallow spiral round the vessel. This cooling water system is also used to cool batched medium sterilized in the vessel prior to its inoculation. 

Ki Antagonist binding affinity Ki67 Nuclear membrane antigen KLH Keyhole limpet haemocyanin K , Michaelis constant KOS KOS strain of herpes simplex... 

Many other devices for use by hand have been invented. Mention may be made of limpet charges which usually employ magnets to make them adhere to the metal sides of tanks or ships. The explosive filling for such charges is a high velocity high power explosive such as cast RDX/TNT. 

The final step is a hydrolyzing step with sulfatase enzymes (E.C. number 3.1.6.1), such as limpet sulfatase, Aerobacter aerogenes sulfatase, Abalone entrail sulfatase, or Helixpomatia sulfatase. This step was suggested to be carried out in a CSTR or fluidized bed reactors, with counter-current flow between the aqueous and the oil phase. A more efficient removal of the sulfate into the aqueous stream is expected to occur in this cross-flow manner. A final separation of the reacting mixture was suggested to obtain sulfur-free product and aqueous enzyme solution for recycle. 

S. Singh, M. Scigelova, and D. H. G. Crout, Glycosidase-catalysed synthesis of mannobioses by the reverse hydrolysis activity of alpha-mannosidase Partial purification of alpha-mannosidases from almond meal, limpets and Aspergillus niger, Tetrahedron Asymmetry, 11 (2000) 223-229. 

Dissolve the protein to be modified at a concentration of 1-10 mg/ml in 0.1 M sodium phosphate, pH 7.4. NaCl may be added to this buffer if desired. For the modification of keyhole limpet hemocyanin (KLH Thermo Fisher) as described by Staros et al., 1986, include 0.9 M NaCl to maintain the solubility of this high-molecular-weight protein. If lower or higher concentrations of the protein are used, adjust the amounts of the other reactants as necessary to maintain the correct molar ratios. 

The most common carrier proteins in use today are keyhole limpet hemocyanin (KLH MW 4.5 X 105 to 1.3 X 107), BSA (MW 67,000), aminoethylated (or cationized) BSA (cBSA), thyroglobulin (MW 660,000), ovalbumin (OVA MW 43,000), and various toxoid proteins, including tetanus toxoid and diphtheria toxoid. Other proteins occasionally used include myoglobin, rabbit serum albumin, immunoglobulin molecules (particularly IgG) from bovine or mouse sera, tuberculin purified protein derivative, and synthetic polypeptides such as poly-L-lysine and poly-L-glutamic acid. 

Senozan, N. et al. (1981) Hemocyanin of the giant keyhold limpet, Megathura crenulata. In Invertebrate Oxygen Binding Proteins Structure, Active Sites, andFunction (J. Lamy, and J. Lamy, eds.), pp. 703-717. Dekker, New York. 

Limpet Latia 535 Luciferine, luciferase, purple protein, 02... 

Common limpet, Patella vulgata-, 10 pg/L for 6 h Brown mussel, Perna indica Pedal mucus production reduced 40% 48... 

Davies, M.S. 1992. Heavy metals in seawater effects on limpet pedal mucus production. Water Res. 26 1691-1693. 

INVERTEBRATES Limpet, Acmaea digitalis California Near bridges ... 

Slipper limpet, Crepidula fornicata Larva LC50 (96 h) 60.0 7... 

---