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PubMed1987

Quantum efficiencies of the reversible photoreaction of octopus rhodopsin.

The classic method of photometric curves for photosensitivity determination has been extended to the case of photoreversible reactions and applied to the octopus rhodopsin --> acid metarhodopsin photoreaction. In such cases, measurements at one irradiation wavelength yield the sum of the photosensitivities of the forward and reverse processes. However, by using different irradiation wavelengths, together with appropriate molar extinction coefficients, the quantum efficiencies for both reactions may be resolved. For detergent-solubilized octopus rhodopsin at room temperature, pH 7, the quantum yields are found to be 0.69 (+/- 0.03) for rhodopsin --> metarhodopsin, in line with values observed in a range of vertebrate visual pigments, and 0.43 (+/- 0.02) for the reverse photoregeneration process. The similarities in overall photosensitivities of the forward and reverse reactions in the visible region are consistent with a significant physiological role for photoreversal in the cephalopod visual cycle.

Animals↗
PubMed1991

A resonance Raman study of octopus bathorhodopsin with deuterium labeled retinal chromophores.

The resonance Raman spectrum of octopus bathorhodopsin in the fingerprint region and in the ethylenic-Schiff base region have been obtained at 80 K using the "pump-probe" technique as have its deuterated chromophore analogues at the C7D; C8D; C8,C7D2; C10D; C11D; C11, C12D2; C14D; C15D; C14, C15D2; and N16D positions. While these data are not sufficient to make definitive band assignments, many tentative assignments can be made. Because of the close spectral similarity between the octopus bathorhodopsin spectrum and that of bovine bathorhodopsin, we conclude that the essential configuration of octopus bathorhodopsin's chromophore is all-trans like. The data suggest that the Schiff base, C = N, configuration is trans (anti). The observed conformationally sensitive fingerprint bands show pronounced isotope shifts upon chromophore deuteration. The size of the shifts differ, in certain cases, from those found for bovine bathorhodopsin. Thus, the internal mode composition of the fingerprint bands differs somewhat from bovine bathorhodopsin, suggesting a somewhat different in situ chromophore conformation. An analysis of the NH bend frequency, the Schiff base C = N stretch frequency, and its shift upon Schiff base deuteration suggests that the hydrogen bonding between the protonated Schiff base with its protein binding pocket is weaker in octopus bathorhodopsin than in bovine bathorhodopsin but stronger than that found in bacteriorhodopsin's bR568 pigment.

Animals↗
PubMed1992

Interaction of rhodopsin, G-protein and kinase in octopus photoreceptors.

Light induced phosphorylation of octopus rhodopsin was greatly enhanced by guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S), suggesting that the kinases are involved in regulating interaction between rhodopsin and G-protein. We determined phosphorylated peptides of octopus rhodopsin in the presence or absence of GTP gamma S. Possible phosphorylation sites for octopus rhodopsin enhanced by GTP gamma S were Thr329, Thr330 and/or Thr336, which suggest that the G-protein associates with cytoplasmic loops including C-terminal peptide in the seventh helix of octopus rhodopsin.

Amino Acid Sequence↗
PubMed1997

Identification of two palmitoyl groups in octopus rhodopsin.

We determined the structure and site of fatty acid incorporated in octopus rhodopsin using a combination of fluorescence label and enzymatic cleavage methods in conjunction with fast-atom bombardment (FAB) mass spectrometry. A single peptide containing two adjacent cysteines, Cys337 and Cys338, was successfully isolated using the fluorescence from a dye conjugated to Cys345. The FAB mass spectrometric analysis of the peptide (323Phe-340Phe) revealed that two palmitoyl groups are linked to Cys337 and Cys338 via thioester bonds in octopus rhodopsin as in bovine rhodopsin.

Amino Acid Sequence↗
PubMed1997

A resonance Raman study of the C=C stretch modes in bovine and octopus visual pigments with isotopically labeled retinal chromophores.

Previous resonance Raman spectroscopic studies of bovine and octopus rhodopsin and bathorhodopsin in the C-C stretch fingerprint region have shown drastically different spectral patterns, which suggest different chromophore-protein interactions. We have extended our resonance Raman studies of bovine and octopus pigments to the C=C stretch region in order to reveal a more detailed picture about the difference in retinal-protein interactions between these two pigments. The C=C stretch motions of the protonated retinal Schiff base are strongly coupled to form highly delocalized ethylenic modes located in the 1500 to 1650 cm-1 spectral region. In order to decouple these vibrations, a series of 11,12-D2-labeled retinals, with additional 13C labeling at C8, C10, C11 and C14, respectively, are used to determine the difference of specific C=C stretch modes between bovine and octopus pigments. Our results show that the C9=C10 and C13=C14 stretch mode are about 20 cm-1 lower in the Raman spectrum of octopus bathorhodopsin than in bovine bathorhodopsin, while the other C=C stretch modes in these two bathorhodopsins are similar. In contrast, only the C9=C10 stretch mode in octopus rhodopsin is about 10 cm-1 lower than in bovine rhodopsin, while other C=C stretches are similar.

Animals↗
PubMed1991

In-vitro interaction of mitomycin C and streptomycin A with collagen.

Mitomycin C and streptomycin A were studied for their interaction with soluble collagens from sepia, fish and rat skins using UV absorption spectroscopy at pH 7.4 and 3.0 and equilibrium dialysis. Both the drugs bound to collagen as shown from association constants and could be quantitatively recovered by prolonged dialysis against water showing formation of dissociable bonds between drug and collagen. At pH 7.4, mitomycin C showed greater binding affinity than streptomycin A with collagen from all three species. The reverse trend was seen at pH 3.0. Binding capacity of sepia and fish skin collagens for streptomycin A at pH 3.0 was found to be significantly greater than for mitomycin C.

Animals↗
PubMed1976

An octopus toxin, maculotoxin, selectively blocks sodium current in squid axons.

1. A low molecular weight, stable, cationic neurotoxin (maculotoxin, MTX) extracted from the posterior salivary glands of the octopus Hapalochlaena maculosa, blocked sodium current in voltage-clamped squid axons without affecting potassium current. 2. The effectiveness of MTX was increased by repetitive, brief, depolarizing pulses but not by a single prolonged depolarization. 3. The potency of MTX decreased at pHs from 8 to 9. Effectiveness could be restored be restored by lowering the pH to 7-1 again. It was concluded that MTX is active in its cationic form. 4. MTX affected sodium conductance kinetics, slowing the turn-on of sodium current. This effect was most noticeable with small deploarizations but became progressively less with larger depolarizations. Neither the turn-off of sodium current nor sodium inactivation kinetics were affected by the toxin. 5. MTX inhibited sodium current without inhibiting sodium gating current. 6. The effectiveness of MTX was not detectably changed when calcium concentration was varied from 50 to 10 mM, or sodium concentration was varied from 225 to 750 mM.

Animals↗
PubMed2001

Control of octopus arm extension by a peripheral motor program.

For goal-directed arm movements, the nervous system generates a sequence of motor commands that bring the arm toward the target. Control of the octopus arm is especially complex because the arm can be moved in any direction, with a virtually infinite number of degrees of freedom. Here we show that arm extensions can be evoked mechanically or electrically in arms whose connection with the brain has been severed. These extensions show kinematic features that are almost identical to normal behavior, suggesting that the basic motor program for voluntary movement is embedded within the neural circuitry of the arm itself. Such peripheral motor programs represent considerable simplification in the motor control of this highly redundant appendage.

Animals↗
PubMed2005

Underwater bipedal locomotion by octopuses in disguise.

Here we report bipedal movement with a hydrostatic skeleton. Two species of octopus walk on two alternating arms using a rolling gait and appear to use the remaining six arms for camouflage. Octopus marginatus resembles a coconut, and Octopus (Abdopus) aculeatus, a clump of floating algae. Using underwater video, we analyzed the kinematics of their strides. Each arm was on the sand for more than half of the stride, qualifying this behavior as a form of walking.

Animals↗
PubMed1974

D(--)-lactic acid and d(--)-lactate dehydrohgenase in octopus spermatozoa.

The spermatozoa of Octopus dofleini martini produce anaerobically D(-)-lactic acid and possess a very active D(-)-lactate dehydrogenase. In this respect, while resembling certain microorganisms, they differ strikingly from mammalian spermatozoa which produce L(+)-lactic acid and contain L(+)-lactate dehydrogenase.

Anaerobiosis↗
PubMed1981

Opioid inhibition of dopamine release from nervous tissue of Mytilus edulis and Octopus bimaculatus.

Morphine and D-Ala2-Met-enkephalin as well as other opioids suppress potassium-stimulated release of 3H-labeled dopamine from neurons tissue of two marine invertebrates, Mytilus edulis and Octopus bimaculatus. Naloxone reverses the inhibitory effects in both species. Potassium-stimulated release of 3H-labeled serotonin is not altered by opioids. It is postulated that opiate receptors and their endogenous effectors play a prominent role in regulation of transmitter release in invertebrates.

Animals↗