Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    The prostaglandin synthesis in marine fish thrombocyte
    Amsterdam : Elsevier
    Comparative Biochemistry and Physiology -- Part B: Biochemistry and 93 (1989), S. 397-402 
    Details
    ISSN: 0305-0491
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0305-0491(89)90098-9
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Calculations of the ground-state correlation energy of the Be atom using multiconfigurational perturbation theory
    Amsterdam : Elsevier
    Chemical Physics Letters 102 (1983), S. 213-215 
    Details
    ISSN: 0009-2614
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0009-2614(83)87394-1
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Purification and characterization of phospholipase A2 from the pyloric caeca of red sea bream, Pagrus major (1997)
    Springer
    Fish physiology and biochemistry 16 (1997), S. 487-498 
    Details
    ISSN: 1573-5168
    Keywords: phospholipase A2 ; red sea bream ; pyloric caeca ; phosphatidylcholine ; bile salts ; calcium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A phospholipase A2 was purified 55,000-fold in a yield of 10% from the lipid-free extract of powder of the pyloric caeca of red sea bream to near homogeneity by sequential column chromatography on S-sepharose fast flow, butyl-cellulofine, Asahipak ES-502C cation-exchange HPLC, TSK gel G3000SW gel-filtration HPLC, and Asahipak ODP-50 reversed-phase HPLC. The final preparation showed a single band with the apparent molecular mass of 14 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis, and an estimated specific activity was 717 µmol min-1 mg-1 protein. The purified enzyme had a pH optimum in the range of pH 8.0–9.0 and required the presence of both 8 mM of Ca2+ and from 2 to 10 mM of sodium deoxycholate for its maximal activity, using 2 mM of phosphatidylcholine as a substrate. The purified enzyme preferentially hydrolyzed the 2-acyl ester bonds of both phosphatidylglycerol and phosphatidylcholine in the presence of sodium deoxycholate, followed in order by phosphatidylethanolamine and phosphatidyl-serine. In contrast to porcine pancreatic PLA2, pyloric caeca PLA2 hydrolyzed mixed-micellar phosphatidylcholine substrate effectively, regardless of the kinds of bile salts used. These results indicate that Ca2+-dependent low molecular mass PLA2, so called secretory PLA2, occurs in the pyloric caeca of red sea beam.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007745021990
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Purification and characterization of bile salt-activated lipase from the hepatopancreas of red sea bream, Pagrus major (1998)
    Springer
    Fish physiology and biochemistry 18 (1998), S. 59-69 
    Details
    ISSN: 1573-5168
    Keywords: red sea bream ; hepatopancreas ; bile salt-activated lipase ; polyunsaturated fatty acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A lipase was purified from the extract of the delipidated powder of red sea bream hepatopancreas to nar homogeneity by fractional precipitation with ammonium sulfate and sequential chromatography on first anion-exchange-, hydrophobic- and second anion-exchange columns followed by gel filtration and anion-exchange HPLC. The final enzyme preparation showed a single band with an apparent molecular mass of approx. 64 kDa by sodium dodecyl sulfate-polyacrylamid e gel electrophoresis. The purified enzyme had a pH optimum in the range of pH 7.0–9.0. Using ρ-nitrophenyl myristate or triolein as a substrate, the enzyme required the presence of sodium taurocholate or sodium cholate for its activity. No activity was observed in the presence of sodium deoxycholate. The enzyme preferentially hydrolyzed ethyl esters of polyunsaturated fatty acid, such as arachidonic acid and eicosapentaenoic acid which were resistant to porcine pancreatic lipase. These results strongly suggest that the enzyme purified from the hepatopancreas of red sea bream is homologous to mammalian bile salt-activated lipase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007725513389
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Presence and ontogeny of intestinal and pancreatic phospholipase A2-like proteins in the Red Sea bream,Pagrus major. An immunocytochemical study (1992)
    Springer
    Fish physiology and biochemistry 9 (1992), S. 427-438 
    Details
    ISSN: 1573-5168
    Keywords: phospholipase A2 ; digestive enzyme ; ontogeny ; red sea bream ; hepatopancreas ; intestine ; pyloric caeca ; immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have studied the location and the ontogeny of the digestive enzyme, phospholipase A2 (PLA2) immunohistochemically in the adult and larvae/juvenile of the red sea breamPagrus major by using an antiserum against theNaja naja venom PLA2. The antiserum reacts with at least one enzyme among the PLA2s purified from the fish hepatopancreas or intestine. Although the reactivities were comparatively low, it labelled zymogen granules of the pancreatic acinar cells and secretory materials of certain epithelial cells in the depths of epithelial crypts in the pyloric caeca of the adult. The immunoreactivities of PLA2s were investigated in the viscera of larvae and juveniles of the 0 to 85th day after hatch. In the larvae of the 13th day, accumulation of PLA2-positive zymogen granules in the pancreatic acinar cells were first recognized by the immunostaining. The intensity of the labelling subsequently became stronger and dramatically increased between the 20th and 30th day. This increase appeared to be one of the physiological changes associated with the transition to a new benthic life as juveniles. Lack of PLA2 in the pancreas before the 13th day may suggest the possibility that larvae utilized exogenous PLA2, inherent in their prey, to digest the phospholipids. On the other hand, no reactivity was found in the intestine until the 85th day.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02274224
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Purification and characterization of phospholipase A2 isoforms from the hepatopancreas of red sea bream, Pagrus major1 (1998)
    Springer
    Fish physiology and biochemistry 18 (1998), S. 135-147 
    Details
    ISSN: 1573-5168
    Keywords: group I phospholipase A2 ; isoforms ; calcium ; hepatopancreas ; marine fish ; Pagrus major
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two phospholipase A2 (PLA2) isoforms, tentatively denoted as DE-1 and DE-2 PLA2s, were purified from the hepatopancreas of red sea bream (Pagrus major) to near homogeneity by sequential column chromatography on S-Sepharose fast flow, DEAE-Sepharose fast flow and butyl-Cellulofine, and by ion-exchange, gel-filtration and reversed-phase HPLC. The purified DE-1 and DE-2 PLA2s both showed a single band with the apparent molecular mass of approx. 13.5 kDa by SDS-polyacrylamide gel electrophoresis, and were found to be both related to group I PLA2 based on the N-terminal amino acid sequences. DE-1 PLA2 had a pH optimum in the alkaline region at around pH 10 and required approximately 10 mM of Ca2+ and 4-10 mM of sodium deoxycholate for its maximal activity, using 2 mM of phosphatidylcholine and phosphatidylethanolamine as substrates. DE-2 PLA2 also had a pH optimum in the alkaline region at around pH 8-9 and required 〉10 mM of Ca2+ and approximately 6 mM of sodium deoxycholate for its maximum activity with 2 mM of phosphatidylcholine as a substrate; its enzymatic activity towards phosphatidylethanolamine was greatly inhibited by the addition of sodium deoxycholate. The results demonstrate that red sea bream hepatopancreas contains two enzymatically distinct group I PLA2 isoforms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007750618685
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Involvement of cytoplasmic pH in the production of ethylene, a potent inducer of sexual development inDictyostelium mucoroides (1991)
    Springer
    Protoplasma 160 (1991), S. 72-76 
    Details
    ISSN: 1615-6102
    Keywords: Dictyostelium mucoroides ; Cellular slime mold ; Cytoplasmic pH ; Ethylene ; Cyclic AMP ; Sexual development ; Macrocyst ; Sorocarp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Dictyostelium mucoroides-7 (Dm 7) and a mutant MF 1 derived from it exhibit two developmental pathways: sorocarp formation occurs during the asexual process, and macrocyst formation during the sexual cycle. The two developmental pathways are mainly regulated by two chemical substances: 3′,5′-cyclic adenosine monophosphate (cAMP) and ethylene. Recently, we have demonstrated that cytoplasmic pH (pHi) has a critical role for the choice of developmental pathways, higher pHi being favourable to macrocyst formation. Thereupon, attention was riveted to the relation of pHi to biosynthesis of cAMP and ethylene. Effect of pHi on the production and release of ethylene, a potent inducer of macrocyst formation, was examined, using the two facing culture method. The result showed that lowered pHi inhibits ethylene production, thus resulting in a failure of cells to form macrocysts. The accumulation of cAMP, an inhibitor of macrocyst formation, was found to vary depending on extracellular pH (pHo), but diethylstilbestrol (DES) that is a proton pump inhibitor and also an inhibitor of macrocyst formation had no significant effect on the accumulation. Taken together these results indicate that higher pHi may induce macrocyst formation through enhancement of ethylene production rather than inhibition of cAMP synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01539958
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...