Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Octopodiformes”

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 487 records · Page 27Linked to original sources

A review of simultaneous visual discrimination as a method of training octopuses.

I have presented a review and critique of the procedures employed in simultaneous discrimination training experiments using octopuses as subjects. Procedural variables were analyzed statistically for their influence on experimental outcome. The variables most significantly associated with successful discriminations included use of a specific start location for subjects, shock as negative reinforcement, fewer trials per session, more sessions per day, and discriminations based on stimulus brightness. No experiment controlled all potential sources of inadvertent cues, and subjects' performances appeared to be sensitive to exact procedural details. The most common practice diminishing evidence for learning involved reward that coincided with the subject's pre-existing preferences. I found no evidence that sub-optimal experimental designs biased experimental outcomes in any significant and systematic way. Although there is sufficient reason for rejecting results of published simultaneous discrimination training experiments, careful conclusive experiments remain to be performed.

Animals↗

Purification and properties of calmodulin-lysine N-methyltransferase from rat brain cytosol.

A S-adenosylmethionine:protein-lysine N-methyltransferase (EC 2.1.1.43) has been purified from rat brain cytosol 7,080-fold with a yield of 8%, using octopus calmodulin as a substrate. It contains a lysine residue that is not fully methylated. The enzyme was purified by ammonium sulfate fractionation, Sephacryl S-200 gel filtration, and phosphocellulose and octopus calmodulin-Sepharose affinity chromatographies. Among protein substrates, it was highly specific toward octupus calmodulin. The Km values for octopus calmodulin and S-adenosyl-L-methionine were found to be 2.2 X 10(-8) M and 0.8 X 10(-6) M, respectively. The molecular weight was estimated to be 57,000 by gel filtration and the pH optimum was between 7.5 and 8.5. The enzyme was stimulated in the presence of 10(-7) M Mn2+ and 10(-4) M Ca2+. HPLC of the acid hydrolysate of methyl-3H-labeled calmodulin showed the formation of epsilon-N-mono, epsilon-N-di, and epsilon-N-trimethyllysine. Reverse-phase HPLC of tryptic peptides of the methyl-3H-labeled calmodulin demonstrated that the labeled N-methyllysine lies in the 107-126 peptide. These findings suggest that this enzyme methylated a specific lysine residue of octopus calmodulin.

Animals↗

Occurrence and some properties of eledoisin in extracts of posterior salivary glands of Eledone.

The posterior salivary glands of Eledone, alone among the tissues of this molluscan species, contain eledoisin, an endecapeptide with activity on blood vessels and extravascular smooth muscles. The salivary glands of Octopus vulgaris and O. macropus lack the polypeptide. Eledoisin is present, in amounts ranging from 20 to 160 mug/g fresh tissue, at all stages of growth and in every season; however, conspicuous differences in the eledoisin content were observed in different groups of animals. Eledoisin is fairly stable in intact salivary glands stored on ice. The most suitable solvent for its extraction is 70 to 80% methanol. Better results are also obtained with boiling diluted acetic acid, than with ethanol, whereas extraction with acetone gives unsatisfactory yields. Eledoisin is stable in neutral or slightly acid medium, but is rapidly destroyed by strong acids and even more rapidly by strong alkalis. It is quickly and completely inactivated by chymotrypsin, and somewhat more slowly and incompletely by trypsin. Carboxypeptidase is ineffective. Passage of crude salivary extracts of Eledone through an alumina column yields preparations of eledoisin which may be considered pure from a biological point of view.

Acetic Acid↗