Disease relevance of Decapodiformes

• The acidosis provoked by octopine formation in Illex was demonstrated to promote the use of the phosphagen and to protect the free energy change of ATP such that the anaerobic scope of metabolism during swimming is extended and expressed more in Illex than in Loligo [1].

High impact information on Decapodiformes

• Identification of the first major allergen of a squid (Todarodes pacificus) [2].
• CONCLUSION: This 38 kd protein is a major allergen of the squid, Todarodes pacificus, and is believed to be squid muscle protein tropomyosin [2].
• Cloning and nucleotide sequence of cDNA for rhodopsin of the squid Todarodes pacificus [3].
• Squid (Todarodes pacificus) retinochrome was reduced to N-retinyl protein with borane dimethylamine and cleaved by CNBr [4].
• The cadmium-binding proteins were shown to exist in the hepatopancreas of three molluscs, a whelk, Buccinum tenuissimum, a turbo, Batillus cornutus, and a squid, Todarodes pacificus [5].

Biological context of Decapodiformes

• A source of large axons for neurophysiology: the North Atlantic squid Illex illecebrosus [6].
• The amino acid sequence of the regulatory light chain of mantle muscle myosin from squid (Todarodes pacificus) was determined by conventional methods [7].

Anatomical context of Decapodiformes

• In the squid parolfactory vesicles (Todarodes pacificus), rhodopsin was present in the central lumen, which contains the distal processes of the photoreceptor cells, while retinochrome was detected in the myeloid bodies scattered within the vesicular wall [8].
• The high molecular weight protein connectin (also called titin) in Japanese common squid (Todarodes pacificus) mantle muscle was identified by western blotting analysis with 3B9, the mouse anti-chicken skeletal muscle connectin monoclonal antibody [9].

Associations of Decapodiformes with chemical compounds

• An empirical equation relating O2 consumption (power input) to pressure production during jet-propelled swimming in the squid (Illex illecebrosus) is compared with hydrodynamic estimates of the pressure-flow power output also calculated from pressure data [10].
• Three fucose-rich glycosaminoglycans (GAGs), illexin A, illexin B and illexin C, were isolated from squid ink of Illex argentinus [11].
• Tyrosinase (monophenol, L-DOPA:oxygen oxidoreductase) was isolated from the ink of the squid, Illex argentinus [12].
• A cysteine-activated protease isolated from todarodes pacificus squid degrades collagen below its denaturation temperature [13].
• Squid (Todarodes pacificus) was sliced, washed, and then salted with 5, 10, and 20% (wt/wt) sodium chloride [14].

Gene context of Decapodiformes

• A cDNA for rhodopsin was isolated from a library constructed from poly(A)+RNA of the squid (Todarodes pacificus) retina [3].
• Anti-IRBP also reacted with pure RALBP prepared from Todarodes pacificus [15].
• Squid (Todarodes pacificus) liver RNase (RNase Tp) was purified [16].
• Comparison of two offshore squid species (Loligo pealei and Illex illecebrosus) with the estuarine squid L.brevis indicates that the latter uses a strategy to delay the exploitation of high-energy phosphates and protect energy levels at higher than the minimum levels (-42 kJ/mol) characterizing fatigue in the other species [17].

Analytical, diagnostic and therapeutic context of Decapodiformes

• Purification, characterization and molecular cloning of tyrosinase from the cephalopod mollusk, Illex argentinus [12].
• A beta-D-galactoside binding lectin (TPL) was newly purified from the body walls of the cuttlefish, Todarodes pacificus with lactosyl-agarose affinity column chromatography and reversed-phase HPLC [18].
• Circular dichroism (CD) and absorption spectra of squid (Todarodes pacificus) rhodopsin, isorhodopsin and the intermediates was measured at low temperatures [19].

References