• Home
  • Search Results
  • Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum.

Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum.

Biochemistry (1985-11-05)
H E Van Wart, D R Steinbrink
ABSTRACT

The substrate specificities of three class I (beta, gamma, and eta) and three class II (sigma, epsilon, and zeta) collagenases from Clostridium histolyticum have been investigated by quantitating the kcat/KM values for the hydrolysis of 53 synthetic peptides with collagen-like sequences covering the P3 through P3 subsites of the substrate. For both classes of collagenases, there is a strong preference for Gly in subsites P1' and P3. All six enzymes also prefer substrates that contain Pro and Ala in subsites P2 and P2' and Hyp, Ala, or Arg in subsite P3'. This agrees well with the occupancies of these sites by these residues in type I collagen. However, peptides with Glu in subsites P2 or P2' are not good substrates, even though Glu occurs frequently in these positions in collagen. Conversely, all six enzymes prefer aromatic amino acids in subsite P1, even though such residues do not occur in this position in type I collagen. In general, the class II enzymes have a broader specificity than the class I enzymes. However, they are much less active toward sequences containing Hyp in subsites P1 and P3'. Thus, the two classes of collagenases have similar but complementary sequence specificities. This accounts for the ability of the two classes of enzymes to synergistically digest collagen.

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 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

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

MilliporeSigma

Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.