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Circular dichroism comparative studies of two bacterial collagenases and thermolysin.

Biochimica et biophysica acta (1980-07-24)
M C Heindl, S Fermandjian, B Keil
RÉSUMÉ

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 fraction of alpha helix, beta sheet and aperiodic segments in the three proteins could be estimated. Good similarity was found between Achromobacter collagenase and thermolysin, which both contain a high fraction of alpha helix. Side-chain contributions were analyzed in the aromatic region of thespectra: effects of pH and of organic solvents were observed, showing the strong influence of surroundings on the stabilization of the proteins.

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Sigma-Aldrich
Collagénase 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
Collagénase from Clostridium histolyticum, for general use, Type I, ≥125 CDU/mg solid
Sigma-Aldrich
Collagénase 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
Collagénase from Clostridium histolyticum, suitable for release of rat epididymal adipocytes and hepatocytes (for methodology see Type II and Type IV), Type VIII, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagénase from Clostridium histolyticum, Type IA, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid, For general use
Sigma-Aldrich
Collagénase from Clostridium histolyticum, Type XI, 2-5 FALGPA units/mg solid, ≥800 CDU/mg solid
Sigma-Aldrich
Collagénase from Clostridium histolyticum, Type V, ≥1 FALGPA units/mg solid, >125 CDU/mg solid
Sigma-Aldrich
Collagénase from Clostridium histolyticum, powder, Suitable for the digestion and isolation of physiologically active pancreatic islet cells, suitable for cell culture
Sigma-Aldrich
Collagénase from Clostridium histolyticum, lyophilized powder, ≥125 CDU/mg solid (CDU = collagen digestion units), 0.5-5.0 FALGPA units/mg solid
Sigma-Aldrich
Collagénase 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
Collagénase from Clostridium histolyticum, lyophilized powder (from 0.2μm filtered solution), 0.5-5.0 FALGPA units/mg solid, suitable for cell culture
Sigma-Aldrich
Collagénase from Clostridium histolyticum, 0.2 μm filtered, suitable for release of physiologically active rat hepatocytes, Type IV-S, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagénase 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
Collagénase from Clostridium histolyticum, lyophilized powder (from 0.2 μm filtered solution), suitable for cell culture
Sigma-Aldrich
Collagénase 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
Collagénase 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
Collagénase from Clostridium histolyticum, 0.2 μm filtered, suitable for release of physiologically active rat epididymal adipocytes, Type II-S, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagénase from Clostridium histolyticum, Sigma Blend Type H, ≥1.0 FALGPA units/mg solid
Sigma-Aldrich
Collagénase from Clostridium histolyticum, non-sterile; 0.2 μm filtered, Type IA-S, 0.5-5.0 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagénase from Clostridium histolyticum, Sigma Blend Type F, ≥2.0 FALGPA units/mg solid
Sigma-Aldrich
Collagénase from Clostridium histolyticum, purified by chromatography, ≥500 CDU/mg solid (CDU = collagen digestion units), lyophilized powder
Sigma-Aldrich
Collagénase from Clostridium histolyticum, 0.2 μm filtered, Type V-S, ≥1 FALGPA units/mg solid, ≥125 CDU/mg solid
Sigma-Aldrich
Collagénase from Clostridium histolyticum, Sigma Blend Type L, ≤1.0 FALGPA units/mg solid