Clostridium histolyticum collagenase

Clostridium histolyticum collagenase. Clostridiopeptidase A. Digestion of native collagen in the triple helical region at Xaa-I-Gly... 

Dheeman DS, Henehan GTM, Frias JM (2011) Purification and properties of Amycolatopsis mediterranei DSM 43304 lipase and its potential in flavour ester synthesis. Bioresour Technol 102 3373-3379 Dive V, Yiotakis A, Nicolaou A, Toma F (1990) Inhibition of Clostridium histolyticum collagenases by phosphonamide peptide inhibitors. Eur J Biochem 191 685-693... 

Collagenase 400 U/ml collagenase from Clostridium histolyticum (high-... 

Some years ago, collagenase from the microorganisms Clostridium histolyticum was shown to be a zinc metalloenzyme 1303 mammalian collagenases are also zinc metalloenzymes.1304 The collagenase-like peptidase of rat testis1305 has also been shown independently to be a zinc metalloenzyme. 

Dipfestion buffer 2 for osteoblast-like cells. Add 200 U/mL of type 1 collagenase from Clostridium histolyticum (Sigma) and 14.7 mg CaCl2 H20 (1 mM) in 100 mL HESS buffer ( ee Notes 1 and 2). 

Islet isolation methods that yield islets free of contaminating fibroblasts now have been developed. Successful prevention of the growth of dense fibrous tissue on extravascular chambers containing these purified islets would raise new possibilities in the design of islet-transplantation chambers. This chapter contains the initial results of binding enzymes to Millipore AA cellulose ester membranes for application in such chambers. The enzyme chosen for study was collagenase from Clostridium histolyticum (Worthington Biochemicals, Inc.). 

The enzyme collagenase is derived from fermentation of Clostridium histolyticum. 

Collagenase a proteolytic enzyme, and the only enzyme capable of degrading native collagen to soluble, low M, peptides. More than 20 C. have been described from baeteiia, fungi, arthropods, amphibia and mammals, C from Clostridium histolyticum and C. from tadpole tail have been extensively studied. Clostridial C (C.A M, 105.000. CB M, 57,000) attacks mainly the peptide bond proceeding the Gly-Pro sequence (-4-Gly(16)-Pro-Ser-4—Gly-Pro-) the bonds in front of Gly-Leu and Gly-Ala are attacked to a lesser extent, e.g. in the a,-chain. 

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