Isolation and expression in Escherichia coli of cslA and cslB, genes coding for the condroitin sulfate-degrading enzymes chondroitinase AC and chondroitinase B, respectively, from Flavobacterium heparinum

Article Abstract:

The genes for two chondroitinases were isolated from Flavobacterium heparinum and expressed in E. coli. Chondroitinase AC has 678 residues and a molecular mass of 77,169 Da; chondroitinase B is 481 residues and 53,563 Da.

Gram-negative bacteria

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Development of a genetic system for the transfer of DNA into Flavobacterium heparinum

Article Abstract:

Research describes the construction of a conjugation/integration plasmid genetic system in Flavobacterium heparinum facilitating the study of the mechanism of enzyme degradation of glycosoaminoglycan by the bacterium.

United States, Physiological aspects, Genetic aspects, Soil microbiology, Bacterial genetics, Conjugation (Biology), Conjugation (Reproduction)

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Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum

Article Abstract:

The genes encoding heparinases II and III (designated hepB and hepC, respectively), containing open reading frames of 2,316 and 1,980 bp, respectively, are apart from each other and from heparinase I. Expression of truncated versions of these genes reveals mature forms of heparinases II and III having 746 and 635 amino acids, respectively, and molecular weights of 84,545 and 73,135, respectively. Expressed at 37 degree C, the enzymes become insoluble and most of the heparinase III protein degraded, whereas expression at 25 degrees C makes them soluble and active.

Analysis, Enzymes, Gene expression, Heparin

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