Fibrinolysin
Identification
- Generic Name
- Fibrinolysin
- DrugBank Accession Number
- DB05254
- Background
Fibrinolysin consists of two polypeptide chains, one light and one heavy, linked by a disulfide bond. The light chain has a molecular weight of approximately 27,000 Da and contains the active center of Fibrinolysin; the heavy chain has a molecular weight of approximately 57,000 Da. Fibrinolysin is used as a local healing ointment when combined together with the enzyme deoxyribonuclease I (extracted from bovine pancreas). Fibrinolysin and deoxyribonuclease both act as lytic enzymes. The combination is available as ointment containing 1 BU (Biological Unit) Fibrinolysin and 666 BUs desoxyribonuclease per gram. The ointment is marketed by Pfizer under the brand name Fibrolan in a variety of countries (e.g. Switzerland). It is currently not approved in the USA.
- Type
- Biotech
- Groups
- Investigational
- Biologic Classification
- Protein Based Therapies
Other protein based therapies - Protein Chemical Formula
- C3848H5912N1096O1185S60
- Protein Average Weight
- 88411.4 Da
- Sequences
>Fibrinolysin heavy chain DLLDDYVNTQGASLLSLSRKNLAGRSVEDCAAKCEEETDFVCRAFQYHSKEQQCVVMAEN SKNTPVFRMRDVILYEKRIYLLECKTGNGQTYRGTTAETKSGVTCQKWSATSPHVPKFSP EKFPLAGLEENYCRNPDNDENGPWCYTTDPDKRYDYCDIPECEDKCMHCSGENYEGKIAK TMSGRDCQAWDSQSPHAHGYIPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPQKRWEFCDI PRCTTPPPSSGPKYQCLKGTGKNYGGTVAVTESGHTCQRWSEQTPHKHNRTPENFPCKNL EENYCRNPNGEKAPWCYTTNSEVRWEYCTIPSCESSPLSTERMDVPVPPEQTPVPQDCYH GNGQSYRGTSSTTITGRKCQSWSSMTPHRHLKTPENYPNAGLTMNYCRNPDADKSPWCYT TDPRVRWEFCNLKKCSETPEQVPAAPQAPGVENPPEADCMIGTGKSYRGKKATTVAGVPC QEWAAQEPHQHSIFTPETNPQSGLERNYCRNPDGDVNGPWCYTMNPRKPFDYCDVPQCES SFDCGKPKVEPKKCSGR
>Fibrinolysin light chain IVGGCVSKPHSWPWQVSLRRSSRHFCGGTLISPKWVLTAAHCLDNILALSFYKVILGAHN EKVREQSVQEIPVSRLFREPSQADIALLKLSRPAIITKEVIPACLPPPNYMVAARTECYI TGWGETQGTFGEGLLKEAHLPVIENKVCNRNEYLDGRVKPTELCAGHLIGGTDSCQGDSG GPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSPYVPWIEETMRRN
Download FASTA Format- Synonyms
- Bovine Fibrinolysin
- Bovine Plasmin
- Fibrinolysin (human)
- Fibrinolysin, human
- Plasmin (bos taurus)
- Plasmin (bovine)
- Plasmin bovine
Pharmacology
- Indication
Fibrinolysin assists with the healing of minor burns, superficial wounds, ulcers, surgical wounds, and superficial hematomas.
Reduce drug development failure ratesBuild, train, & validate machine-learning modelswith evidence-based and structured datasets.Build, train, & validate predictive machine-learning models with structured datasets.- Contraindications & Blackbox Warnings
- Prevent Adverse Drug Events TodayTap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.Avoid life-threatening adverse drug events with our Clinical API
- Pharmacodynamics
Not Available
- Mechanism of action
Fibrinolysin attacks and inactivates fibrin molecules occurring in undesirable exudates on the surface of the human body and on human mucosa, e.g., in superficial wounds and burns, while desoxyribonuclease targets and destroys (human) DNA. The combination of the two enzymes has a synergistic effect on necrotic but not on living tissue.
Target Actions Organism UPlasminogen activator inhibitor 1 Not Available Humans UUrokinase-type plasminogen activator Not Available Humans - Absorption
Not Available
- Volume of distribution
Not Available
- Protein binding
Not Available
- Metabolism
local inactivation
- Route of elimination
Not Available
- Half-life
Almost completely inactivated after 24 hours.
- Clearance
Not Available
- Adverse Effects
- Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.
- Toxicity
Not Available
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs Browse all" title="About SNP Mediated Effects/ADRs" id="snp-actions-info" class="drug-info-popup" href="javascript:void(0);">
- Not Available
Interactions
- Drug Interactions Learn More" title="About Drug Interactions" id="structured-interactions-info" class="drug-info-popup" href="javascript:void(0);">
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.
Drug Interaction Integrate drug-drug
interactions in your softwareCitalopram The risk or severity of bleeding can be increased when Fibrinolysin is combined with Citalopram. Desvenlafaxine The risk or severity of adverse effects can be increased when Desvenlafaxine is combined with Fibrinolysin. Inotersen The risk or severity of thrombocytopenia can be increased when Inotersen is combined with Fibrinolysin. Levomilnacipran The risk or severity of bleeding can be increased when Fibrinolysin is combined with Levomilnacipran. Olive oil The therapeutic efficacy of Fibrinolysin can be decreased when used in combination with Olive oil. - Food Interactions
- No interactions found.
Products
- Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.
- International/Other Brands
- Elase (Pfizer) / Fibrolan (Pfizer)
Categories
- ATC Codes
- B01AD05 — Fibrinolysin
- B01AD — Enzymes
- B01A — ANTITHROMBOTIC AGENTS
- B01 — ANTITHROMBOTIC AGENTS
- B — BLOOD AND BLOOD FORMING ORGANS
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- Not Available
- Kingdom
- Organic Compounds
- Super Class
- Organic Acids
- Class
- Carboxylic Acids and Derivatives
- Sub Class
- Amino Acids, Peptides, and Analogues
- Direct Parent
- Peptides
- Alternative Parents
- Not Available
- Substituents
- Not Available
- Molecular Framework
- Not Available
- External Descriptors
- Not Available
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- D60E3WIF5Y
- CAS number
- 9004-09-5
References
- Synthesis Reference
U.S. Patent 2,624,691; U.S. Patent 3,136,703; U.S. Patent 3,234,106.
- General References
- Birk Y, Khalef S, Jibson MD: Purification and properties of protease F, a bacterial enzyme with chymotrypsin and elastase specificities. Arch Biochem Biophys. 1983 Sep;225(2):451-7. [Article]
- External Links
Clinical Trials
- Clinical Trials Learn More" title="About Clinical Trials" id="clinical-trials-info" class="drug-info-popup" href="javascript:void(0);">
Phase Status Purpose Conditions Count
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Ointment Cutaneous - Prices
- Not Available
- Patents
Patent Number Pediatric Extension Approved Expires (estimated) Region US2624691 No 1953-01-06 1980-01-06 US US3136703 No 1964-06-09 1981-06-09 US US3234106 No 1966-02-08 1983-02-08 US
Properties
- State
- Liquid
- Experimental Properties
- Not Available
Targets
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Serine-type endopeptidase inhibitor activity
- Specific Function
- Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major con...
- Gene Name
- SERPINE1
- Uniprot ID
- P05121
- Uniprot Name
- Plasminogen activator inhibitor 1
- Molecular Weight
- 45059.695 Da
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Serine-type endopeptidase activity
- Specific Function
- Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
- Gene Name
- PLAU
- Uniprot ID
- P00749
- Uniprot Name
- Urokinase-type plasminogen activator
- Molecular Weight
- 48507.09 Da
Drug created at November 18, 2007 18:09 / Updated at February 21, 2024 02:33