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Th1047 details
Primary information
ID1331
ThPP IDTh1047
Therapeutic Peptide/Protein NameAlpha-1-proteinase inhibitor
SequenceEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNI view full sequnce in fasta
Functional ClassificationIIa
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting Point (℃)59
Half LifeN.A.
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of Distribution5632 ± 2006 mL [ARALAST NP]
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesSerine Proteinase Inhibitors
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionN.A.
TargetNeutrophil elastase
Information of corresponding available drug in the market
Brand NameAralast
CompanyBaxter
Brand DiscriptionARALAST is an Alpha-1 proteinase inhibitor. ARALAST contains approximately 67% Alpha-PI with the C-T-terminal lysine truncation.
Prescribed forIts used to treat lung problems (emphysema) caused by a certain inherited disease (alpha-1-proteinase inhibitor deficiency). In people with this condition, lung damage is caused by elastase, a natural substance that the body needs to kill bacteria in the
Chemical NameN.A.
FormulationARALAST NP is available as a lyophilized powder in single dose vials containing 0.5 gram or 1 gram of functional Alpha 1 -Protenase inhibitor
Physcial AppearanceLyophilized powder
Route of AdministrationIntravenous infusion
Recommended DosageRecommended dose is 60 mg/kg of body weight, administered once in a week.
ContraindicationARALAST NP is contraindicated in immunoglobulin A deficient patients with antibodies against IgA, due to the risk of severe hypersensitivity.
Side EffectsFever, chills, body aches, flu symptoms, sores in your mouth and throat; pain or burning when you urinate; wheezing, chest pain or tightness, trouble breathing; or vision changes.
Useful Linkhttp://www.baxter.com/downloads/healthcare_professionals/products/Aralast_NP_PI.pdf
PubMed ID16773239
3-D StructureTh1047 (View) or (Download)
Primary information
ID1332
ThPP IDTh1047
Therapeutic Peptide/Protein NameAlpha-1-proteinase inhibitor
SequenceEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNI view full sequnce in fasta
Functional ClassificationIIa
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting Point (℃)59
Half LifeN.A.
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of Distribution5618 ± 1618 mL [Aralast]
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesTrypsin Inhibitors
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionN.A.
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsNausea, bloating; headache, dizziness, drowsiness; feeling tired; back pain, joint or muscle pain; swelling in your hands or feet; flushing (warmth, redness, or tingly feeling); cold symptoms such as stuffy nose, sneezing, sore throat, cough; or mild itch
Useful Linkhttp://www.drugs.com/mtm/aralast.html
PubMed ID16773239
3-D StructureTh1047 (View) or (Download)
Primary information
ID1333
ThPP IDTh1047
Therapeutic Peptide/Protein NameAlpha-1-proteinase inhibitor
SequenceEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNI view full sequnce in fasta
Functional ClassificationIIa
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting Point (℃)59
Half LifeN.A.
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesEnzyme Replacement Agents
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionN.A.
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful Linkhttp://www.webmd.com/drugs/2/drug-74919/aralast-iv/details
PubMed ID16773239
3-D StructureTh1047 (View) or (Download)
Primary information
ID1334
ThPP IDTh1047
Therapeutic Peptide/Protein NameAlpha-1-proteinase inhibitor
SequenceEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNI view full sequnce in fasta
Functional ClassificationIIa
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting Point (℃)59
Half LifeN.A.
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionN.A.
TargetN.A.
Information of corresponding available drug in the market
Brand NameProlastin
CompanyTalecris Biotherapeutics C formerly Bayer
Brand DiscriptionProlastin (alpha) is a sterile, stable, lyophilized preparation of purified human Alpha1-Proteinase Inhibitor (alpha1-PI), also known as alpha1-antitrypsin. Prolastin (alpha) is prepared from pooled human plasma of normal donors by modification and refine
Prescribed forIt is used to treat alpha 1-antitrypsin deficiency in people who have symptoms of emphysema.
Chemical NameN.A.
FormulationThe specific activity of Prolastin is _ 0.35 mg functional alpha1-PI/mg protein and when reconstituted as directed, the concentration of alpha1-PI is _ 20 mg/mL. When reconstituted, Prolastin (alpha) has a pH of 6.6_7.4, a sodium content of 100_210 mEq/L,
Physcial AppearanceLyophilized powder
Route of AdministrationIntravenous infusion
Recommended DosageProlastin (alpha) may be given at a rate of 0.08 mL/kg/min or greater and must be administered intravenously. The recommended dosage of 60 mg/kg takes approximately 30 minutes to infuse.
ContraindicationIndividuals with selective IgA deficiencies who have known antibody against IgA (anti-IgA antibody) should not receive Alpha1-Proteinase Inhibitor (Human), Prolastin (alpha) , since these patients may experience severe reactions, including anaphylaxis, to IgA which may be present.
Side EffectsFever, chills, body aches, flu symptoms, sores in your mouth and throat; pain or burning when you urinate; wheezing, chest pain or tightness, trouble breathing; or vision changes.
Useful Linkhttp://www.prolastin.com/
PubMed ID16773239
3-D StructureTh1047 (View) or (Download)
Primary information
ID1335
ThPP IDTh1047
Therapeutic Peptide/Protein NameAlpha-1-proteinase inhibitor
SequenceEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNI view full sequnce in fasta
Functional ClassificationIIa
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting Point (℃)59
Half LifeN.A.
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionN.A.
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsNausea, bloating; headache, dizziness, drowsiness; feeling tired; back pain, joint or muscle pain; swelling in your hands or feet; flushing (warmth, redness, or tingly feeling); cold symptoms such as stuffy nose, sneezing, sore throat, cough; or mild itching.
Useful Linkhttp://www.drugs.com/mtm/prolastin.html
PubMed ID16773239
3-D StructureTh1047 (View) or (Download)
Primary information
ID1336
ThPP IDTh1047
Therapeutic Peptide/Protein NameAlpha-1-proteinase inhibitor
SequenceEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNI view full sequnce in fasta
Functional ClassificationIIa
Molecular Weight44324.5
Chemical FormulaC2001H3130N514O601S10
Isoelectric Point5.37
Hydrophobicity-0.302
Melting Point (℃)59
Half LifeN.A.
DescriptionHuman alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation.
Indication/DiseaseFor treatment of panacinar emphysema.
PharmacodynamicsPrevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema.
Mechanism of ActionAlpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
ToxicityN.A.
MetabolismN.A.
AbsorptionN.A.
Volume of DistributionN.A.
Clearance940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg]
CategoriesN.A.
Patents NumberN.A.
Date of IssueN.A.
Date of ExpiryN.A.
Drug InteractionN.A.
TargetN.A.
Information of corresponding available drug in the market
Brand NameN.A.
CompanyN.A.
Brand DiscriptionN.A.
Prescribed forN.A.
Chemical NameN.A.
FormulationN.A.
Physcial AppearanceN.A.
Route of AdministrationN.A.
Recommended DosageN.A.
ContraindicationN.A.
Side EffectsN.A.
Useful Linkhttp://www.rxlist.com/prolastin-drug.htm
PubMed ID16773239
3-D StructureTh1047 (View) or (Download)