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  • Biochemistry and Biotechnology  (2)
  • Key words: Octocoral, diterpene, antifouling, furan, lactone, barnacles, cypris settlement  (1)
  • peptides  (1)
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Material
Years
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Antisettlement and Narcotic Action of Analogues of Diterpene Marine Natural Product Antifoulants from Octocorals (1999)
    Springer
    Marine biotechnology 1 (1999), S. 427-436 
    Details
    ISSN: 1436-2236
    Keywords: Key words: Octocoral, diterpene, antifouling, furan, lactone, barnacles, cypris settlement
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract: Prevoius studies have determined that the octocorals Renilla reniformis and Leptogorgia virgulata contain diterpenes that are potent inhibitors of barnacle settlement. These antifoulants—the renillafoulins and pukalide—are, however, comparatively complex and thus are not amenable to commercial exploitation. The present study examined 19 analogues, based on the functional groups of lactone and furan rings in the parent molecules, for antisettlement activity and toxicity. The latter parameters are presented as EC50 values for inhibition of cypris settlement and naupliar swimming, respectively. Assays of a subset of the analogues indicated that they were active in solution rather than when bound to a surface and that at relatively high concentrations they had a narcotic action. The mechanism whereby some of the analogues were able to inhibit settlement at nontoxic concentrations has yet to be explained but suggests that there is merit in the present approach to antifoulant development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/PL00011799
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Macromolecular cues in marine systems (1986)
    Springer
    Journal of chemical ecology 12 (1986), S. 1013-1023 
    Details
    ISSN: 1573-1561
    Keywords: Marine animals ; macromolecules ; peptides ; glycoproteins ; behavior ; prey detection ; site selection ; metamorphosis ; biopolymers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A review of the roles of biopolymers as marine chemical cues is presented. The goal of the review is to provide a context within which to view present research and to provide insight into future research potential for macromolecules in marine chemical ecology. The roles of peptides, proteins, glycoproteins, proteoglycans, lectins, and mucopolysaccharides are discussed. Biological events mediated include: larval settlement and metamorphosis, gamete attraction, predator-prey interactions, alarm responses, feeding responses, nonfood resource acquisition, trail following, and larval-release behavior. Molecular origins, transmission, modulation, and multifunctionality of cues are discussed and illustrated with specific examples. The advantages of biopolymers, especially peptides and proteins, as specific cues in marine systems derive from their solubility, specific information content (due to the asymmetric nature of the monomer and the wordlike information content of the primary structure of the polymer), distance transmission in water by bulk flow rather than diffusion, relatively high signal-to-noise ratio, and common occurrence as structural and metabolic components of all living organisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01638993
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences (1994)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 19 (1994), S. 302-309 
    Details
    ISSN: 0887-3585
    Keywords: dinuclear copper site ; hemocyanin ; oxygen binding ; allosteric regulation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The X-ray structure of an oxygenated hemocyanin molecule, subunit II of Limulus polyphemus hemocyanin, was determined at 2.4 Å resolution and refined to a crystallographic R-factor of 17.1%. The 73-kDa subunit crystallizes with the symmetry of the space group R32 with one subunit per asymmetric unit forming hexamers with 32 point group symmetry. Molecular oxygen is bound to a dinuclear copper center in the protein's second domain, symmetrically between and equidistant from the two copper atoms. The copper-copper distance in oxygenated Limulus hemocyanin is 3.6 ± 0.2 Å, which is surprisingly 1 Å less than that seen previously in deoxygenated Limulus polyphemus subunit II hemocyanin (Hazes et al., Protein Sci. 2:597, 1993). Away from the oxygen binding sites, the tertiary and quaternary structures of oxygenated and deoxygenated Limulus subunit II hemocyanins are quite similar. A major difference in tertiary structures is seen, however, when the Limulus structures are compared with deoxygenated Panulirus interruptus hemocyanin (Volbeda, A., Hol, W. G. J. J. Mol. Biol. 209:249, 1989) where the position of domain 1 is rotated by 8° with respect to domains 2 and 3. We postulate this rotation plays an important role in cooperativity and regulation of oxygen affinity in all arthropod hemocyanins. © 1994 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340190405
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Functional properties of hemoglobin immobilized in coacervates prepared from gelatin A and polyanionic carbohydrates (1990)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 35 (1990), S. 831-836 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Complex coacervation is a phenomenon of phase separation that may occur in a solution of positively and negatively charged polyions. The resulting two phases are distinguished by the total concentration of both polyions, with the concentrated phase often containing vesicular structures composed of the two polyelectrolytes. We have used this phenomenon in an attempt to-prepare a hemoglobin-based red blood cell analog. Hemoglobin-containing coacervate vesicles have been prepared from gelatin A and the polyanionic carbohydrates acacia, pectin, or dextranstilfate. Hemoglobin seems to be anchored into the vesicle walls through interaction of its polyanion binding site with the negatively charged residues on the carbohydrates. Oxygen binding by the immobilized HbA is reversible and cooperative, with p50 values at 20°C of 2.8, 6, and 24 mm Hg for the acacia- (pH 7.5), pectin- (pH 6.6), and dextransulfate-(pH 6.6) derived coacervates. Kinetic studies on CO binding show that the rate of CO uptake by the coacervates (t½ = 13-27 ms at 0.5 mM CO) is similar to that of human erythrocytes.The HbA-containing coacervates slowly dissolve in isotonic salt solutions (145 mM NaCl, pH 7.4), but they can be stabilized by treatment with glutaraldehyde. Oxygen binding by HbA incorporated into the stabilized coacervates derived from dextran sulfate is very similar to oxy gen binding by human red blood cells: p50 = 26 mm Hg and n = 1.89 at 37°C in isotonic salt. These results show how a novel approach, based on an old concept, has led to the preparation of immobilized HbA, with functional properties similar to those of intraerythrocytic HbA.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260350811
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    Paper (German National Licenses)
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