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Literature summary for 1.14.18.1 extracted from

  • Hata, S.; Azumi, K.; Yokosawa, H.
    Ascidian phenoloxidase: its release from hemocytes, isolation, characterization and physiological roles (1998), Comp. Biochem. Physiol. B, 119, 769-776.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1-Phenyl-2-thiourea
-
Halocynthia roretzi
diethyldithiocarbamate 2 mM, complete inhibition, 1 mM Cu2+ restores activity to original level Halocynthia roretzi
DL-dithiothreitol 0.1 mM, complete inhibition Halocynthia roretzi
L-cysteine 0.1 mM, 86% inhibition Halocynthia roretzi
Metabisulfite 0.1 mM, 99% inhibition, 1 mM Cu2+ restores activity to original level Halocynthia roretzi
Na2S2O4 0.1 mM, 30% inhibition Halocynthia roretzi

Metals/Ions

Metals/Ions Comment Organism Structure
copper
-
Halocynthia roretzi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
gel filtration Halocynthia roretzi
62000
-
1 * 62000, SDS-PAGE Halocynthia roretzi

Organism

Organism UniProt Comment Textmining
Halocynthia roretzi
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Sp-Sephadex, Sephadex G-100 Halocynthia roretzi

Source Tissue

Source Tissue Comment Organism Textmining
hemocyte enzyme is released in response to foreign materials such as sheep red blood cells and yeast cells as well as to allogenic hemocytes Halocynthia roretzi
-

Subunits

Subunits Comment Organism
monomer 1 * 62000, SDS-PAGE Halocynthia roretzi