Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Decapodiformes”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 433 records · Page 24Linked to original sources

A comparison of the effect of experimental general anaesthetics on nerve impulse blockade and on a proteinaceous target site.

While it has been reported that general anaesthetics inhibit the enzyme luciferase and thus reduce the light output of the reaction with luciferin, we find that in squid giant axons injected with luciferin and luciferase, treatment with experimental general anaesthetics at concentrations sufficient to block axonal conduction leads to an increase in the light production by the reaction. This potentiation of the protein activity is best observed when luciferin concentration is above the apparent association constant. Our findings raise doubts regarding the suitability of luciferase as a model for the target region of general anesthetic action.

Action Potentials↗

Proposed tertiary structure of the sodium channel.

On the basis of our recent results of the complete amino acid sequence of the squid Loligo bleekeri sodium channel deduced by cloning and sequence analysis of the complementary DNA (Sato, C. and Matsumoto, G. Biochem. Biophys. Res. Comm. 186, 1), we have proposed a tertiary structure model of the sodium channel where the transmembrane segments are octagonally aligned and the four linkers of S5-6 between segments S5 and S6 play a crucial role in the activation gate, voltage sensor and ion selective pore, which can slide, depending on membrane potentials, along inner walls consisting of segments S2 and S4 alternately. The proposed model is contrasted with that of Noda et al. (Nature 320; 188-192, 1986).

Amino Acid Sequence↗

Polyclonal antibody generation in rabbit by administration of an organophosphorus acid anhydrolase (OPAA) from squid.

When a nerve gas hydrolyzing enzyme [organophosphorus acid anhydrolase (OPAA), formerly DFPase] purified from squid hepatopancreas was injected into rabbits, the resulting sera (RAS) inhibited OPAA purified from either squid hepatopancreas or squid optic ganglia. The inhibition was non-competitive, with 50% inhibition at a 1:1,000 serum dilution, and with the limit of inhibition (in effect, a "titer") at approximately 1:10,000. This RAS did not inhibit the distinctly different OPAAs from a mammalian and two bacterial sources. The hepatopancreas-generated RAS also reacted positively to the appropriate enzyme-linked immunosorbent assay (ELISA) at a titer of 1:100,000. In marked contrast, when OPAA purified from squid optic ganglion was injected into rabbits, the resulting sera did not inhibit squid OPAA, and did not give a positive ELISA. Control sera taken from the same rabbits prior to any injection (RS) did not inhibit the OPAAs. These results show another major difference between squid type OPAAs and the OPAAs from other sources, sometimes termed "Mazur type" OPAAs.

Animals↗