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Literature summary for 3.4.21.86 extracted from

  • Nakamura, T.; Morita, T.; Iwanaga, S.
    Intracellular proclotting enzyme in limulus (Tachypleus tridentatus) hemocytes: its purification and properties (1985), J. Biochem., 97, 1561-1574.
    View publication on PubMed
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Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
 inactive proenzyme, 1 * 54000, active enzyme, 1 * 25000 + 1 * 31000, SDS-PAGE Tachypleus tridentatus
31000
-
 inactive proenzyme, 1 * 54000, active enzyme, 1 * 25000 + 1 * 31000, SDS-PAGE Tachypleus tridentatus
54000
-
 SDS-PAGE, absence of 2-mercaptoethanol Tachypleus tridentatus

Organism

Organism UniProt Comment Textmining
Tachypleus tridentatus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein 11% carbohydrate content, contains 11 and 10 residues of glucosamine and galactosamine, resp Tachypleus tridentatus
additional information does not contain gamma-carboxyglutamic acid Tachypleus tridentatus
proteolytic modification inactive proenzyme of 54 kDa is converted to its active form of 25 kDa + 31 kDa by purified factor B or by trypsin. Heavy and light chain of active form are bridged by a disulfide linkage Tachypleus tridentatus

Purification (Commentary)

Purification (Comment) Organism
-
 Tachypleus tridentatus

Source Tissue

Source Tissue Comment Organism Textmining
hemocyte hemocyte lysate Tachypleus tridentatus
-

Subunits

Subunits Comment Organism
dimer inactive proenzyme, 1 * 54000, active enzyme, 1 * 25000 + 1 * 31000, SDS-PAGE Tachypleus tridentatus
More serine active site of enzyme is within the heavy chain Tachypleus tridentatus