Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.10.3.1 (tyrosinase)
 9,065 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Galactosamine-induced fulminant hepatic failure rats were used for in vivo studies of the removal of tyrosine and total free phenol by means of hemoperfusion over immobilized tyrosinase within artificial cells. The elevated plasma tyrosine level was decreased to about half the value after one hour of hemoperfusion. The studies of tyrosine clearance suggest that it is efficient and remains constant throughout the one-hour hemoperfusion. In those galactosamine-induced fulminant hepatic failure rats with increased total free phenol levels hemoperfusion over tyrosinase artificial cells significantly lowered the level.
 ...
PMID:Tyrosinase immobilized within artificial cells for detoxification in liver failure: II. In vivo studies in fulminant hepatic failure rats. 679 85

A 66-kDa lectin (OmA) was purified from the serum of the Yucatan peninsula endemic octopus (Octopus maya) by a single step affinity chromatography on glutaraldehyde-fixed stroma from rat erythrocytes. OmA corresponds to 0.8% of the total circulating protein in the hemolymph; it is composed of three equal subunits of 22kDa each, and 7.4% of linked carbohydrates. The amino acids' composition indicated that agglutinin contained mainly aspartic and glutamic acids, and cysteine and methionine were identified in minor proportion. OmA agglutinates mainly rat, guinea pig, and rabbit erythrocytes, and this activity is partially inhibited by galactosamine, melobiose, galacturonic acid, mannose, and methyl alpha and beta galactosides. Hemagglutinating activity is not dependent on divalent cations, such as Ca(2+), Mg(2+), or Mn(2+). The OmA subunits showed no identity for any lectin in databases but partial identity with the type A hemocyanin from Octopus dolfleini hemolymph; the main similarities are related to tyrosinase domains and copper A and B sites that conform to the oxygen-binding site of hemocyanin.
 ...
PMID:Purification and partial characterization of an agglutinin from Octopus maya serum. 2010 60