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C8176

Sigma-Aldrich

Collagenase from Clostridium histolyticum

Sigma Blend Type L, ≤1.0 FALGPA units/mg solid

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Synonym(s):
Clostridiopeptidase A
CAS Number:
9001-12-1
Enzyme Commission number:
3.4.24.3 (BRENDA, IUBMB)
EC Number:
232-582-9
MDL number:
MFCD00130830
NACRES:
NA.54

Quality Level

200

form

powder

caseinase activity

≥40 units/mg solid

specific activity

≤1.0 FALGPA units/mg solid

mol wt

68-130 kDa

storage temp.

−20°C

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Application

Collagenase from Clostridium histolyticum, or Clostridiopeptidase A, has been used in a study to assess the synthesis and in vitro evaluation of macromolecular antitumour derivatives based on phenylenediamine mustard. Clostridiopeptidase A has also been used in a study to investigate the enzymatic debridement of burn wounds with collagenase.

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. Ethylene glycol-bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid (EGTA)4; β-mercaptoethanol; glutathione, reduced; thioglycolic acid, sodium; and 2,2′-dipyridyl; 8-hydroxyquinoline are known to inhibit the enzyme activity.
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.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

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

Regulatory Information

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N I Solov'eva et al.
Bioorganicheskaia khimiia, 20(3), 303-309 (1994-03-01)
Interactions of collagenases I and II (clostridiopeptidases) from Clostridium histolyticum with hexapeptide substrates in which some L-proline residues are replaced by their D-analogues, as well as with the tripeptide chloromethyl ketone Z-Gly-Pro-Gly-CH2Cl were studied. A role of stereochemistry of the
Coşkun Ozcan et al.
Burns : journal of the International Society for Burn Injuries, 28(8), 791-794 (2002-12-05)
Seventy-eight pediatric burn patients treated by enzymatic debridement with collagenase clostridiopeptidase A (CCA), were compared to 41 patients those burn wounds were excised surgically. Patients whose burn wounds were initially assessed as partial-thickness at admission were enrolled in the study.
Dag K Skovseth et al.
Methods in molecular biology (Clifton, N.J.), 360, 253-268 (2006-12-19)
The future ability to manipulate the growth of new blood vessels (angiogenesis) holds great promise for treating ischemic disease and cancer. Several models of human in vivo angiogenesis have been described, but they seem to depend on transgenic support and
Katleen De Winne et al.
European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences, 24(2-3), 159-168 (2005-01-22)
Poly-[N-(2-hydroxyethyl)-L-glutamine] (PHEG) and poly(ethylene glycol) (PEG)-grafted PHEG conjugates of N,N-di(2-chloroethyl)-4-phenylenediamine mustard (PDM) were synthetised. A collagenase-sensitive oligopeptide spacer was selected to link the cytotoxic agent PDM onto the polymeric carrier. First, the oligopeptide-drug conjugate, L-pro-L-leu-gly-L-pro-gly-PDM, was prepared. In a second
Agata Kurzyk
Methods in molecular biology (Clifton, N.J.), 2429, 417-434 (2022-05-05)
Evaluation of mesenchymal stem cell seeding efficiency in three-dimensional (3D) scaffolds is a critical step for constructing a potent and useful tissue engineering product for regenerative medicine. To determine the quantity of cells seeded on a scaffold, their condition and
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Protocols

Enzymatic Assay of Collagenase (EC 3.4.24.3) using FALGPA (N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala)

To measure collagenase activity, N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala is used in a continuous spectrophotometric rate determination at 345 nm. Collagenase hydrolyzes collagen peptide bonds.

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