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Characterization of the individual collagenases from Clostridium histolyticum.

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

The six collagenases (alpha, beta, gamma, delta, epsilon, and zeta) from Clostridium histolyticum isolated in the preceding paper [Bond, M. D., & Van Wart, H. E. (1984) Biochemistry (first paper of three in this issue)] have been characterized in detail. The molecular weights determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis range from 68 000 to 125 000. Isoelectric focusing experiments demonstrate that the isoelectric points of the collagenases are in the 5.35-6.20 range. These experiments also reveal that the subspecies of alpha- and gamma-collagenases (alpha1 vs. alpha 2 and gamma 1 vs. gamma 2) have different isoelectric points but the same molecular weights. Microheterogeneity is also observed for the beta- and epsilon-collagenases. The amino acid compositions of all six collagenases have been determined, and analysis for neutral sugars and hexosamines shows that none of the enzymes have a significant carbohydrate content. Zinc and calcium are the only metals that copurify with the collagenases. The purified enzymes contain approximately 1 mol of zinc/mol of protein and a calcium content that varies from about 2 mol/mol for alpha-collagenase to about 7 mol/mol for beta-collagenase. All of the collagenases are 5-10 times more active against gelatin than collagen. The alpha-, beta-, and gamma-collagenases are significantly less active toward the synthetic peptide substrates examined than the delta-, epsilon, and zeta-collagenases. This property, taken together with data on the stabilities and amino acid compositions of these enzymes, strongly supports their assignment to two distinct classes. This establishes clearly that C. histolyticum does, indeed, produce more than one different type of collagenase.

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
Roche
Collagenase A, from Clostridium histolyticum
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 0.2 μm 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, non-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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