C4785
Collagenase from Clostridium histolyticum
0.2 μm filtered, release of physiologically active rat pancreatic islets tested, Type XI-S, 2-5 FALGPA units/mg solid, >1200 CDU/mg solid
Synonym(s):
Clostridiopeptidase A
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sterility
0.2 μm filtered
form
lyophilized powder
specific activity
>1200 CDU/mg solid
2-5 FALGPA units/mg solid
mol wt
68-130 kDa
suitability
release of physiologically active rat pancreatic islets tested
storage temp.
−20°C
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Biochem/physiol Actions
Effective release of cells from tissue requires the action of collagenase enzymes and the neutral protease. Collagenase is activated by four gram atom calcium (Ca2+) per mole enzyme. The culture filtrate is thought to contain at least 7 different proteases ranging in molecular weight from 68-130 kDa. The pH optimum is 6.3-8.8. The enzyme is typically used to digest the connective components in tissue samples to liberate individual cells. Collagenase treatment can cause some cells to die. Typically, concentrations varying from 0.1 to 5 mg/mL are used for digestion. The duration of reaction varies from 15 minutes to several hours and yields a satisfactory efficiency of cell dissociation without causing too much cell death. Krebs Ringer buffer with calcium and BSA is preferred and Zn2+ is required for activity. This enzyme is tested for suitability for the release of hepatocytes (at approx. 1 mg/mL in a total volume of 100 mL) for each rat liver.
Collagenase is activated by four gram atom calcium per mole enzyme. It is inhibited by ethylene glycol-bis(beta-aminoethyl ether) - N, N, N′,N′-tetraacetic acid, beta-mercaptoethanol, glutathione, thioglycolic acid and 8-hydroxyquinoline.
Unit Definition
One collagen digestion unit (CDU) liberates peptides from collagen from bovine achilles tendon equivalent in ninhydrin color to 1.0 μmole of leucine in 5 hours at pH 7.4 at 37 °C in the presence of calcium ions. One FALGPA hydrolysis unit hydrolyzes 1.0 μmole of furylacryloyl-Leu-Gly-Pro-Ala per min at 25°C. One Neutral Protease unit hydrolyzes casein to produce color equivalent to 1.0 μmole of tyrosine per 5 hr at pH 7.5 at 37°C. One Clostripain Unit hydrolyzes 1.0 μmole of BAEE per min at pH 7.6 at 25°C in the presence of DTT.
Preparation Note
Also contains clostripain, nonspecific neutral protease, and tryptic activities.
Prepared from Type XI (C7657)
substrate
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Jörg Witthaut et al.
Clinical drug investigation, 31(11), 791-798 (2011-10-05)
Injectable collagenase Clostridium histolyticum is efficacious in correcting Dupuytren's contracture as assessed by changes in the angle of contracture and range of motion (ROM). However, clinically important changes in ROM have not been evaluated in depth. The objective of this
A Endo et al.
Journal of biochemistry, 102(1), 163-170 (1987-07-01)
A collagenase active against native, insoluble collagen was isolated from the culture filtrate of a streptomycete which has been designated Streptomyces sp. C-51. Collagenase was produced by growing this strain in media containing gelatin. Purification by ammonium sulfate fractionation and
M D Bond et al.
Biochemistry, 23(13), 3092-3099 (1984-06-19)
The relationship between the six collagenases (alpha, beta, gamma, delta, epsilon, and zeta) isolated and characterized in the preceding papers [Bond, M.D., & Van Wart, H.E. (1984) Biochemistry (preceding two papers in this issue)] has been investigated. Chemical modification reactions
M C Heindl et al.
Biochimica et biophysica acta, 624(1), 51-59 (1980-07-24)
The recently isolated and purified collagenase produced by Achromobacter iophagus, the collagenase from Clostridium histolyticum, and thermolysin, three enzymes having common properties, were studied by circular dichroism. From the spectra of the aqueous solutions obtained in the peptide region, the
Jörg Witthaut et al.
The Journal of hand surgery, 38(1), 2-11 (2012-12-12)
The JOINT I (United States) and JOINT II (Australia and Europe) studies evaluated the efficacy and safety of collagenase clostridium histolyticum (CCH) injection for the treatment of Dupuytren contracture. Both studies used identical open-label protocols. Patients with fixed-flexion contractures of
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