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Production and characterization of monoclonal antibodies against Panulirus interruptus hemocyanin.
Biological chemistry Hoppe-Seyler, 1995 Since the primary and higher-order structures of hemocyanin from the crustacean arthropod Panulirus interruptus have been elucidated completely, it should be possible to determine which regions of this immunogenic molecule are recognized most often by antibodies.
PERTON, FG +3 more
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Multiple linkage in Panulirus interruptus hemocyanin
Biochemistry, 1979Emilia Chiancone +2 more
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Panulirus Interruptus Hemocyanin
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984The amino-acid sequence of a part of Panulirus interruptus hemocyanin subunit a comprising the three ligands of the first copper ion has been determined. By fitting this sequence to the electron density map (Gaykema W.P.J.; Hol, W.G.J.; Vereijken J.M; Soeter N.M.; Bak H.J.; Beintema J.J.
Johan M. Vereijken +2 more
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Structure of Panulirus interruptus hemocyanin at 5 Å resolution
Journal of Molecular Biology, 1982The hemocyanin from the spiny lobster Panulirus interruptus, a hexamer with a molecular weight of approximately 540,000, was crystallized in space group P21 with two molecules in the unit cell and cell dimensions a = 119.8 A, b = 193.1 A, c = 122.2 A and β = 118.1 °.
VANSCHAICK, EJM +4 more
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Serum lipoproteins in the spiny lobster, Panulirus interruptus
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 19781. Most of the lipids in the hemolymph of the spiny lobster, Panulirus interruptus, were associated with a high density lipoprotein (HDL3). The lipid of this lipoprotein was composed of phospholipid (88%), sterol (4%) and triglyceride (3%). 2. In animals fed 14C-labeled triglyceride radioactivity was not seen in the serum until 12 hr after feeding ...
R F, Lee, D L, Puppione
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Characterization of eight polymorphic microsatellite loci for the California spiny lobster, Panulirus interruptus and cross-amplification in other achelate lobsters [PDF]
Conservation Genetics Resources, 2009 Microsatellite sequences were isolated from both non-enriched and enriched genomic libraries of California spiny lobster, Panulirus interruptus. Eight consistently amplifying, scorable and polymorphic loci were characterized for 79 individuals collected ...
Tal Ben-Horin +2 more
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Feeding ecology of juvenile spiny lobster, Panulirus interruptus, on the Pacific coast of Baja California Sur, Mexico [PDF]
New Zealand Journal of Marine and Freshwater Research, 2005 Many aspects of the early life history of the red lobster Panulirus interruptus are little known, including the relationship between habitat structure, food resource availability, and nutrition of juveniles.
Mark Butler, Elisa Servière Zaragoza
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Fish & Shellfish Immunology, 2003
In the spiny lobster (Panulirus interruptus), unlike other crustaceans most of the prophenoloxidase (proPO) was detected in cell-free plasma (86.3%). In spite of its location, lobster proPO activating system has a similar activation mechanism to other crustacean proPO systems.
Jorge, Hernández-López +4 more
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In the spiny lobster (Panulirus interruptus), unlike other crustaceans most of the prophenoloxidase (proPO) was detected in cell-free plasma (86.3%). In spite of its location, lobster proPO activating system has a similar activation mechanism to other crustacean proPO systems.
Jorge, Hernández-López +4 more
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Heterogeneity of Panulirus interruptus Hemocyanin
1977Panulirus interruptus hemocyanin is heterogeneous both at the level of undissociated and dissociated protein. It is possible to fractionate dissociated protein into three components with different chromatographic and electrophoretic properties. Investigations on the structural differences probably cause the observed heterogeneity.
A. A. Van Den Berg +2 more
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Influence of antibody binding on oxygen binding behavior of Panulirus interruptus hemocyanin
FEBS Letters, 1997 Oxygen binding behavior of monomeric subunit a and the hexameric form of this subunit of hemocyanin of Panulirus interruptus is influenced by the binding of various monoclonal antibodies.
Heinz Decker, J J Beintema
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