|
| Primary information |
|---|
| ID | 10435 |
| Therapeutic ID | Th1074 |
| Protein Name | Alglucerase |
| Sequence | >Th1074_Alglucerase
ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ
|
| Molecular Weight | 55597.4 |
| Chemical Formula | C2532H3854N672O711S16 |
| Isoelectric Point | 7.41 |
| Hydrophobicity | -0.168 |
| Melting point | NA |
| Half-life | 3.6-10.4 min |
| Description | Human Beta-glucocerebrosidase or Beta-D-glucosyl-N-acylsphingosine glucohydrolase E.C. 3.2.1.45. 497 residue protein with N-linked carbohydrates. Alglucerase is prepared by modification of the oligosaccharide chains of human Beta-glucocerebrosidase. The modification alters the sugar residues at the non-reducing ends of the oligosaccharide chains of the glycoprotein so that they are predominantly terminated with mannose residues |
| Indication/Disease | For the treatment of Gaucher's disease (deficiency in glucocerebrosidase) |
| Pharmacodynamics | Gaucher disease is characterized by a functional deficiency in Beta-glucocerebrosidase enzymatic activity and the resultant accumulation of lipid glucocerebroside in tissue macrophages which become engorged and are termed Gaucher cells. Gaucher cells are typically found in liver, spleen and bone marrow. This can lead to an enlarged spleen and liver (hepatosplenomegaly). Secondary hematologic sequelae include severe anemia and thrombocytopenia. Injections of alglucerase into Gaucher disease patients leads to elevated serum levels of the enzyme and reduction in the accumulation of glucocerebroside |
| Mechanism of Action | Alglucerase catalyzes the hydrolysis of the glycolipid, glucocerebroside, to glucose and ceramide as part of the normal degradation pathway for membrane lipids. |
| Toxicity | NA |
| Metabolism | NA |
| Absorption | NA |
| 49.4 to 282.1 mL/kg |
| Clearance | NA |
| Categories | Alimentary Tract and Metabolism,Enzyme Replacement Therapy,Enzymes,Enzymes and Coenzymes,Gaucher Disease,Glucosidases,Glycoside Hydrolases,Hydrolases,Hydrolytic Lysosomal Glucocerebroside-specific Enzyme,Recombinant Proteins |
| Patents Number | NA |
| Date of Issue | NA |
| Date of Expiry | NA |
| Drug Interaction | NA |
| Target | Glucocerebroside |
| Brand Name | NA |
| Company | NA |
| Brand Description | NA |
| Prescribed For | NA |
| Chemical Name | NA |
| Formulation | NA |
| Physical Appearance | NA |
| Route of Administration | NA |
| Recommended Dosage | NA |
| Contraindication | NA |
| Side Effects | NA |
| Useful Link 1 | NA |
| Useful Link 2 | NA |
| Remarks | NA |