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PubMed1984

Purification and characterization of four different alkaline phosphatases from Spirographis spallanzanii.

Alkaline phosphatases (APs) present in Spirographis spallanzanii were extracted by water homogenization of butanol treatment. The enzymes solubilized as above were purified by acetone fractionation and then by DEAE-cellulose and Sephadex G-200 chromatography; separation of four AP forms was achieved, which were characterized by studying their molecular and catalytic properties. The various APs differ in molecular weight, electrophoretic mobility, optimum pH, but show similar Km values and substrate inhibition pattern. Kinetic studies carried out with several inhibitors show, in particular, the existence in these APs of a second binding site and suggest a possible role for them in the metabolism of phosphoric esters of the sugars.

Alkaline Phosphatase↗
PubMed1984

Quantitative semi-automated enzymatic assay for tissue glycogen.

A simple, rapid, specific and reproducible assay for tissue glycogen is described. The method involves the incubation of a denatured tissue homogenate with amyloglucosidase resulting in the complete hydrolysis of glycogen to glucose. The glucose content of the homogenate supernatant is then determined with the aid of a glucose analyzer. The method has been used to measure the glycogen content of a variety of discrete and complex animal tissues and is particularly convenient for microdeterminations.

Animals↗
PubMed1987

Isolation from lugworm (Arenicola cristata) of four proteases that activate cyclic AMP phosphodiesterase.

1. Four cyclic AMP phosphodiesterase-activating activities, designated as A, B, C and D, were isolated from lugworm, Arenicola cristata, by preparative flat-bed isoelectric focusing. Activators C and D were further purified by TSK 3000SW HPLC to homogeneity. 2. Activators A, B, C, and D corresponded to pIs of 4.4, 5.0, 5.2 and 5.4; their mol wts were estimated to be 36,200, 30,500, 30,200 and 28,300 respectively. 3. The protease nature of these activities were confirmed by the inhibition by several trypsin inhibitors of their activation of phosphodiesterase and by their hydrolysis of TAME, a synthetic trypsin substrate. Only protease A also hydrolyzed BTEE, a chymotrypsin substrate.

3',5'-Cyclic-AMP Phosphodiesterases↗
PubMed1989

Purity of Glycera dibranchiata monomer hemoglobin components III and IV determined by isoelectric focusing.

1. The Glycera dibranchiata monomer hemoglobin components III and IV display behavior upon high voltage isoelectric focusing which is similar, but not identical to the behavior demonstrated by monomer hemoglobin component II (Constantinidis and Satterlee (1987). Biochemistry 26, 7779-7786). 2. Both components III and IV show multiple line behavior and formation of significant amounts of apoprotein when solutions of each holoprotein are focused on polyacrylamide gels. 3. The apoprotein of each component focuses as a single line, indicating that this is the most unambiguous estimate of purity for these proteins. 4. The purity of the component III and IV preparations can be estimated to be at least 95%.

Animals↗
PubMed1990

Characterization and peptidase specificity of lugworm (Arenicola cristata) protease C.

1. Lugworm protease C further purified by benzamidine-affinity chromatography, exhibited peptidase specificity for arginyl and lysyl bonds. 2. Protease C consisted of a single polypeptide with a mol. wt of ca 23,000 as determined by SDS polyacrylamide gel electrophoresis, exhibited a u.v. absorption maximum at 280 with an (mg/ml) extinction coefficient of 0.93 and fluorescence spectra typical of a protein containing tryptophan, and had an amino acid composition similar to trypsins. 3. The Kms of the cleavages of the arginyl bond of oxidized insulin B chain and of the lysyl bond of the gly23-ala30 fragment were determined to be 0.72 and 0.96 mM; the corresponding kcats were 38 sec-1 and 1.5 sec-1. The Km and kcat for TAME were 0.042 mM, and 110 sec-1. 4. Lugworm protease C was confirmed to be a trypsin.

Amino Acid Sequence↗
PubMed1996

Oxygen binding properties of Eudistylia vancouverii chlorocruorin and its dodecamer subunit.

The oxygen equilibrium curves of the extracellular chlorocruorin of the polychaete Eudistylia vancouverii and its dodecamer subunit were determined over the pH range from 7.1 to 8.1 and in the presence and absence of 100 mM Mg2+. Although the chlorocruorin has a very low oxygen affinity, high cooperativity and a moderate alkaline Bohr effect (P50 = 145 mmHg, nmax = 6.9, phi = -0.44 at pH 7.1 and 25 degrees C), the dodecamer subunit has higher affinity and lower cooperativity and Bohr coefficient (P50 = 58 mmHg, nmax = 1.7, phi = -0.22). The presence of 100 mM Mg2+ increased the oxygen affinity and cooperativity of the chlorocruorin but had no significant effect on the dodecamer subunit. The oxygen binding properties of the chlorocruorin reassociated subsequent to complete dissociation in 4 M urea at neutral pH were similar to the properties of the dodecamer and not to those of the native chlorocruorin. Fitting to the Monod-Wyman-Changeux allosteric model gave KT of 0.0013 mmHg-1, Kr of 0.22 mmHg-1 and L(o) of 2.5 x 10(13) together with a size of the allosteric unit, N = 9.

Animals↗
PubMed1991

Synthesis and characterization of a recombinant myohemerythrin protein encoded by a synthetic gene.

The antigenic epitopes of the myohemerythrin (MHr) molecule have been studied extensively. The critical amino acid residues responsible for its immune recognition have been identified by using synthetic peptides and the technique of epitope scanning. To assess the true relevance of these techniques for determining the molecular mechanism of antigenic recognition and immunogenicity, the results obtained with isolated peptides should be tested in the context of the folded protein. To this end, we have designed and constructed a synthetic MHr gene, in modular form, which will allow subsequent alterations of nucleotide sequence encoding epitopes of interest. We have produced the recombinant protein at high level, and have shown by several criteria that it possesses the chemical, physical and immunological properties of the native worm protein. Thus, we have developed a valuable system for detailed immunological studies of the structure and chemistry required for antibody binding to protein.

Amino Acid Sequence↗
PubMed1984

Neuromuscular pharmacology of the anterior intestine of Chaetopterus variopedatus, a filter-feeding polychaete.

The motricity of the anterior intestine of Chaetopterus variopedatus was investigated using extracellular electrodes, force displacement transduction and a pharmacological approach. Rhythmic bursts of impulses were associated with peristaltic waves; the latter were not abolished by removal of the ventral nerve cord which caused a drop in tonus. Acetylcholine induced a contracture and an increase in the frequency of peristaltic waves; these effects were potentiated by eserine and reduced by atropine. Similar responses to adrenaline and noradrenaline were antagonized by propranolol and phentolamine in partially different manners. Gamma-aminobutyric acid (GABA) induced large, picrotoxin-sensitive contractures but failed to change the rate of peristalsis. Serotonin (5-HT) produced a short-term increase in the rate of peristalsis as well as a slight contracture, and a long-term inhibition of peristalsis, all actions antagonized by methysergide. The response to GABA was reduced or abolished during the inhibitory phase of the 5-HT effect. A tetrapeptide related to cholecystokinin/gastrin induced contractures and accelerated peristalsis at a concentration as low as 2.5 X 10(-13) M. It is concluded that multiple neurotransmitter pathways may modulate gut motricity by acting on the peristalsis pacemaker as well as on neuromuscular transmission mechanisms.

Animals↗
PubMed1992

Quinacrine-staining of neurones, and activity of purine nucleosides and nucleotides in marine and terrestrial invertebrates from several phyla.

1. The acridine derivative quinacrine was used to stain nerve fibres in internal organs of 17 species of marine and terrestrial invertebrates from seven different phyla. 2. The majority of preparations showed quinacrine-stained nerve fibres. There was a degree of variation, ranging from a dense network of nerve bundles to single fibres. Quinacrine-positive nerve cell bodies were also observed in some ganglia. 3. Pharmacological experiments were performed on a variety of isolated tissues from the different marine and terrestrial groups, in order to ascertain their sensitivity to adenine nucleosides and nucleotides. 4. Correlation is drawn between the ability of neurones within a tissue to bind quinacrine, and the ability of that tissue to respond to applied adenine nucleosides and nucleotides.

Animals↗
PubMed1992

The localization of FMRFamide in the nervous and somatic tissues of Nereis virens and its effects upon the isolated esophagus.

1. The tetrapeptide FMRFamide which is present in extracts of Nereis virens was localized in various nereid tissues immunohistochemically. 2. Immunoreactive FMRFamidergic cells and fibers were found in the supraesophageal (brain) and subesophageal ganglia, as well as in the intersegmental ganglia of the ventral nerve cord. Immunoreactive fibers were present in the neuropile of, and the connectives between, the supraesophageal, subesophageal, and intersegmental ganglia. 3. In the periphery immunoreactive FMRFamidergic fibers and a few cell bodies were observed in the gut. Sparse fibers were also seen in the body wall, parapodia, and cephalic palps. When the antiserum was preabsorbed with FMRFamide, no specific immunoreactivity was detected. 4. The esophagus of Nereis, isolated and suspended in a tissue bath, responded to FMRFamide with a dose-dependent relaxation; threshold was between 30 and 300 nM, and the EC50 was 1.55 +/- 0.60 microM. Benzoquinonium did not modify this response. 5. Thus, FMRFamide seems to be a neurotransmitter in both the central and peripheral nervous system of Nereis virens, and may be involved in the control of esophageal motility.

Animals↗
PubMed1993

Pharmacological evidence for the presence of a beta-adrenoceptor-like agonist in the amphinoid polychaete Eurythoe complanata.

1. Methanolic extracts from the body wall of Eurythoe complanata (ExEc) were tested for biological activity on the isolated rat ileum. 2. ExEc produced either relaxation or relaxation followed by contraction of the rat ileum in a concentration-dependent manner. 3. The predominant relaxation response to ExEc was completely blocked by the beta-adrenoceptor antagonist propranolol and was unaffected by the alpha-adrenoceptor antagonist phenoxybenzamine. 4. The results indicate that the relaxation induced by ExEc is mediated by beta-adrenoceptors. The presence of a myorelaxing substance in E. complanata that selectively activates the beta-adrenoceptors is suggested.

Adrenergic beta-Agonists↗
PubMed1993

Erythrocyte membrane structural features that are critical for the lytic reaction of Spirograhis spallanzani coelomic fluid hemolysin.

1. Hemolytic activity of Spirographis spallanzani coelomic fluid depends on factor(s) strongly influenced by calcium but not by sulfhydril or disulfide reagents. 2. The lytic reaction was suppressed by low zinc ion concentrations but it was not influenced by the presence of proteinase inhibitors. 3. These data indicate that S. spallanzani hemolysin is a non-enzymatic, calcium-dependent, zinc-inhibitable factor that occurs naturally in the coelomic fluid. 4. In the absence of calcium, enzymatic desialization converted sheep erythrocytes into susceptible targets, suggesting the involvement of erythrocyte surface sialic acid. 5. However, the inhibitory effect of the sugar on anti-rabbit lysis was partially removed by addition of calcium. 6. Attempts to characterize membrane components that are critical for hemolysis were performed by inhibition experiments. 7. We found that saccharides, glycoproteins, mucosubstances as well as rabbit erythrocyte soluble tryptic fragments were ineffective in inhibiting hemolysis. 8. Sonicated dispersion of phosphatidyl choline, phosphatidyl glycerol, phosphatidyl ethanol, sphingomyelin and cholesterol did not influence the hemolytic reaction. 9. Rabbit erythrocyte extracted from membrane lipids (chloroform phase) did not modify the lytic activity against rabbit red blood cells. 10. Conversely, the methanol phase consistently reduced the lytic capacity of the fluid. 11. The heat-stable, trypsin-resistant inhibitory factor was most probably a small molecule, since dialysis removed the inhibitory effect.

Animals↗
PubMed1995

Isolation and characterization of four novel bioactive peptides from a polychaete annelid, Perinereis vancaurica.

Four bioactive peptides were purified from an extract of the polycheate annelid Perinereis vancaurica using an HPLC system for fractionation of the extract and the esophagus of the worm as bioassay system. The sequences of the peptides were determined to be H-Trp-Val-Val-Gly-Asp-Val-Gln-OH, H-Ala-Thr-Trp-Leu-Asp-Thr-OH, H-Trp-Met-Val-Gly-Asp-Val-Gln-OH and H-Phe-Tyr-Glu-Gly-Asp-Val-Pro-Tyr-OH. These peptides showed an excitatory activity on the esophagus of P. vancaurica. The excitatory effect of the second and fourth peptides was marked. They may be neuropeptides involved in regulation of the esophagus.

Amino Acid Sequence↗
PubMed1988

Changes in the protein components of vitelline envelope during oogenesis of a tubiculous polychaete, Schizobranchia insignis.

In sabellid polychaetes the vitelline envelopes, in which microvilli with glycocalyx structures at the tips are invested, change in structure during oogenesis. Vitelline envelopes isolated from Schizobranchia oocytes 25-100 micron and 160-185 micron in diameter, were analyzed in protein components by iodination, electrophoresis, Western blotting and radioactive labeling technique. The observations demonstrate that the membrane proteins of the vitelline envelopes are not consistent but variable in components during oogenesis. Most of these proteins, particularly the high molecular weight proteins, are PAS-positive glycoproteins, which may have specific carbohydrate residues binding to wheat germ agglutinin. The proteins could be labeled with [3H]valine within 36 h by incubating the whole oocytes in sea water to a high level, indicating that the proteins are actively synthesized by the growing oocytes. Synthetic rates of the proteins differ from each other at one stage and are higher in the small than in the large oocytes in general, suggesting that the membrane proteins are involved in the function of the vitelline envelopes during oogenesis.

Animals↗
PubMed2006

Role of melanin in mechanical properties of Glycera jaws.

The remarkable mechanical prowess of the jaws of the bloodworm Glycera dibranchiata appears to be a consequence of a robust cross-linked network of organic molecules, notably melanin and proteins, as well as small amounts of unmineralized Cu and a Cu-based mineral. The present study focuses on the role of melanin. Mechanical properties of untreated jaws and the constituent melanin are probed through nanoindentation, both in air and underwater. Complementary information is obtained from density and porosity measurements and attempts at Cu removal from the jaws using EDTA, an effective metal chelator in most biological systems. In near-tip regions of the jaws, mechanical properties attain the highest values and diminish only slightly when wet (by 15-25%), in contrast to the behavior of other organic biomaterials. The melanin constituent contributes significantly to the mechanical integrity of the jaw; its hardness and elastic modulus are about half those of untreated jaws. Although melanin may be the dominant shape-determining component of the structure, it remains to be shown whether jaw assembly is mediated by protein deposition on a melanin scaffold or, conversely, by melanin deposition on a protein scaffold. The inability of EDTA to chelate Cu from the jaws and the relatively high density of the jaws and the melanin support the notion of a highly cross-linked molecular structure. Finally, based on the metric H(3)/E(2) (H being hardness and E the Young's modulus), the results suggest that the abrasion resistance of the jaws is superior to all engineering polymers and competitive with the hardest metallic alloys.

Animals↗
PubMed2005

Experimental results on bioaccumulation of metals and organic contaminants from marine sediments.

A test-system for the assessment of bioavailability and bioaccumulation of metals and organic contaminants in marine benthic organisms is described and results from studies where this system has been applied are assessed. Sediments tested were polluted harbour sediment (from Norway), and clean sediments spikes with metal containing weight materials for drilling muds. Contaminants that may bioaccumulate under relevant conditions are indicated. The test-system uses two species of ecological relevance (Nereis diversicolor and Hinia reticulata). Interspecies differences in bioaccumulation were found for several compounds, which show the importance of using species with different modes of living in such tests. Compared to other PAHs, pyrene was found to bioaccumulate to a high degree (BioAccumulation Ratio, BAR=213.5>sediment concentration ratio, SCR=97.4; bioaccumulation factor, organism dw. conc. to sediment dw. conc., BAF=1.02), which shows that extrapolating bioaccumulation results between different substances is difficult. When assessing bioavailability of specific compounds, it is most adequate to perform direct measurements on exposed organisms, such as the experiments described here. The high bioaccumulation of compounds such as pyrene and nickel may in some cases be attributed to manipulation of the sediments and (for pyrene) lack of subsequent aging, thereby overestimating bioavailability.

Animals↗
PubMed2005

Differences in PAH tolerance between Capitella species: underlying biochemical mechanisms.

The polychaete Capitella capitata consists of a species complex within which differences in tolerance to toxicants have been observed. For example, it has been shown that Capitella sp. S is more sensitive (e.g., in terms of survival, growth and reproduction) to PAH and other stressors than the more opportunistic Capitella sp. I, which is able to take up and biotransform the PAH fluoranthene (Flu). In the present study, an investigation was performed to examine whether differences in tolerance between Capitella species sp. I and sp. S are due to differences in biotransformation, measured as the amount of Flu-metabolites produced by worms. We exposed both sibling species to sediment contaminated with 21 and 26 microg Flu/g dry weight sed for 10--15 days. We found that Capitella sp. I took up more Flu from the sediment than sp. S (346 microg Flu eq./g dry weight worm versus 219 microg Flu eq./g dry weight worm, respectively), but as sp. I was much more effective at biotransforming this PAH (62% versus 11%, respectively of total Flu), the net amounts of parent Flu accumulated by the two species were similar. We found significant differences in the subcellular distribution of Flu and its metabolites between sibling species, with sp. I accumulating mostly in the cytosol and sp. S accumulating mostly in the membrane fraction. A previous study by our group showed Flu to be genotoxic to sp. I upon biotransformation. In the present study, we found no detectable genotoxicity in sp. S following Flu exposure. Our results demonstrate that DNA damage is tightly coupled to biotransformation ability and that other aspects of PAH toxicity (e.g., membrane disruption) are more relevant than DNA damage for predicting tolerance differences between these species.

Analysis of Variance↗