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Relationship between the individual collagenases of Clostridium histolyticum: evidence for evolution by gene duplication.

Biochemistry (1984-06-19)
M D Bond, H E Van Wart
ABSTRACT

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 establish that all six enzymes contain essential carboxyl, tyrosine, and lysine residues. Circular dichroism spectra of the peptide bond region show that the secondary structures of the collagenases are very similar. Ouchterlony double-immunodiffusion experiments carried out with antiserum prepared against beta-collagenase indicate that all six collagenases are cross-reactive. Reverse-phase high-pressure liquid chromatography elution profiles of tryptic digests of these collagenases and sodium dodecyl sulfate electrophoresis gels of the peptides formed on reaction with cyanogen bromide have been obtained. The results indicate that the class I collagenases have extensive sequence homology with each other and that the class II collagenases have extensive sequence homology with each other but that the enzymes in the two classes have substantially different sequences. In addition, the data show that beta-collagenase probably consists of domains that have homologous amino acid sequences, which may have arisen by full or partial intragenic gene duplication. This may account for the unusually high molecular weight of this and the other collagenases. Finally, on the basis of the similarities between the collagenases in the two classes, it is suggested that one class evolved from the other by gene duplication followed by independent evolution by point mutations to yield enzymes with different substrate specificities.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Collagenase from Clostridium histolyticum, suitable for release of physiologically active rat hepatocytes, Type IV, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, for general use, Type I, 0.25-1.0 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, suitable for release of physiologically active rat epididymal adipocytes, Type II, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, release of rat epididymal adipocytes and hepatocytes tested (for methodology see Type II and Type IV), Type VIII, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, Type IA, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid, For general use
Sigma-Aldrich
Collagenase from Clostridium histolyticum, release of physiologically active rat pancreatic islets tested, Type XI, 2-5 FALGPA units/mg solid, ≥800 CDU/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, powder, Suitable for the digestion and isolation of physiologically active pancreatic islet cells, suitable for cell culture
Sigma-Aldrich
Collagenase from Clostridium histolyticum, lyophilized powder, ≥125 CDU/mg solid (CDU = collagen digestion units), 0.5-5.0 FALGPA units/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, release of physiologically active rat pancreatic islets tested, Type V, ≥1 FALGPA units/mg solid, >125 CDU/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, 0.2 μm filtered, release of physiologically active rat hepatocytes tested, Type IV-S, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, high purity, purified by chromatography, Type VII, ≥4 FALGPA units/mg solid, lyophilized powder, ≥700 CDU/mg solid (CDU = collagen digestion units)
Sigma-Aldrich
Collagenase from Clostridium histolyticum, lyophilized powder (from 0.2μm filtered solution), 0.5-5.0 FALGPA units/mg solid, suitable for cell culture
Sigma-Aldrich
Collagenase from Clostridium histolyticum, lyophilized powder (from sterile-filtered solution), Suitable for digestion and isolation of physiologically active pancreatic islet cells, suitable for cell culture
Sigma-Aldrich
Collagenase from Clostridium histolyticum, 0.2 μm filtered, release of physiologically active rat epididymal adipocytes tested, Type II-S, 0.5-5.0 FALGPA units/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, 0.2 μm filtered, for general use, Type I-S, 0.2-1.0 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, sterile; 0.2 μm filtered, Type IA-S, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, 0.2 μm filtered, high purity, purified by chromatography, Type VII-S, ≥4 FALGPA units/mg solid, ≥700 CDU/mg solid (CDU = collagen digestion units)
Sigma-Aldrich
Collagenase from Clostridium histolyticum, Sigma Blend Type F, ≥2.0 FALGPA units/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, Sigma Blend Type H, ≥1.0 FALGPA units/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, powder, suitable for cell culture, ≥4 FALGPA units/mg solid, high purity, ≥700 CDU/mg solid (CDU = collagen digestion units)
Sigma-Aldrich
Collagenase from Clostridium histolyticum, 0.2 μm filtered, suitable for release of physiologically active rat pancreatic islets, Type V-S, ≥1 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagenase from Clostridium histolyticum, purified by chromatography, ≥0.25 FALGPA units/mg solid, ≥250 CDU/mg solid (CDU = collagen digestion units), lyophilized powder
Sigma-Aldrich
Collagenase from Clostridium histolyticum, Sigma Blend Type L, ≤1.0 FALGPA units/mg solid

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