Fibrinolysin

Identification

Name
Fibrinolysin
Accession Number
DB05254
Description

Fibrinolysin (also known as bovine plasmin) is a bovine enzyme derived from bovine plasma or extracted from bacterial cultures. It is a globular protein with a molecular weight of ~90,000 daltons. 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.

Contraindications & Blackbox Warnings
Learn about our commercial Contraindications & Blackbox Warnings data.
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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.

TargetActionsOrganism
UPlasminogen activator inhibitor 1Not AvailableHumans
UUrokinase-type plasminogen activatorNot AvailableHumans
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
Learn about our commercial Adverse Effects data.
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Toxicity
Not Available
Affected organisms
  • Humans and other mammals
Pathways
Not Available
Pharmacogenomic Effects/ADRs
Not Available

Interactions

Drug Interactions
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.
DrugInteraction
AbciximabThe risk or severity of bleeding can be increased when Abciximab is combined with Fibrinolysin.
AceclofenacThe risk or severity of bleeding and hemorrhage can be increased when Aceclofenac is combined with Fibrinolysin.
AcemetacinThe risk or severity of bleeding and hemorrhage can be increased when Acemetacin is combined with Fibrinolysin.
AcenocoumarolThe risk or severity of bleeding can be increased when Acenocoumarol is combined with Fibrinolysin.
Acetylsalicylic acidAcetylsalicylic acid may increase the anticoagulant activities of Fibrinolysin.
Albutrepenonacog alfaThe therapeutic efficacy of Albutrepenonacog alfa can be decreased when used in combination with Fibrinolysin.
AlclofenacThe risk or severity of bleeding and hemorrhage can be increased when Alclofenac is combined with Fibrinolysin.
AldesleukinThe risk or severity of bleeding can be increased when Fibrinolysin is combined with Aldesleukin.
AlemtuzumabThe risk or severity of bleeding can be increased when Fibrinolysin is combined with Alemtuzumab.
AlteplaseThe risk or severity of bleeding can be increased when Fibrinolysin is combined with Alteplase.
Additional Data Available
  • Extended Description
    Extended Description

    Extended description of the mechanism of action and particular properties of each drug interaction.

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  • Severity
    Severity

    A severity rating for each drug interaction, from minor to major.

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  • Evidence Level
    Evidence Level

    A rating for the strength of the evidence supporting each drug interaction.

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  • Action
    Action

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Food Interactions
No interactions found.

Products

International/Other Brands
Elase (Pfizer) / Fibrolan (Pfizer)

Categories

ATC Codes
B01AD05 — FibrinolysinB06AA02 — Fibrinolysin and desoxyribonuclease
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

Chemical Identifiers

UNII
A4028U842W
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
  1. 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. [PubMed:6226244]
PubChem Substance
347910050
RxNav
4388
Wikipedia
Plasmin

Clinical Trials

Clinical Trials
PhaseStatusPurposeConditionsCount

Pharmacoeconomics

Manufacturers
Not Available
Packagers
Not Available
Dosage Forms
Not Available
Prices
Not Available
Patents
Patent NumberPediatric ExtensionApprovedExpires (estimated)Region
US2624691No1953-01-061980-01-06US flag
US3136703No1964-06-091981-06-09US flag
US3234106No1966-02-081983-02-08US flag
Additional Data Available
  • Filed On
    Filed On

    The date on which a patent was filed with the relevant government.

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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 on November 18, 2007 11:09 / Updated on September 19, 2020 20:19

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