Enzymic degradation of heparin. A glucosaminidase and a glycuronidase from Flavobacterium heparinum

Biochemistry ◽  
1969 ◽  
Vol 8 (5) ◽  
pp. 2089-2094 ◽  
Author(s):  
Carl P. Dietrich
Keyword(s):  
Flavobacterium Heparinum

scholarly journals Treatment of Bovine Nasal Cartilage Proteoglycan with Chondroitinases from Flavobacterium heparinum and Proteus vulgaris

1972 ◽  
Vol 247 (14) ◽  
pp. 4521-4528 ◽  
Author(s):  
Vincent C. Hascall ◽  
Rick L. Riolo ◽  
James Hayward ◽  
Clifford C. Reynolds
Keyword(s):  
Proteus Vulgaris ◽  
Nasal Cartilage ◽  
Cartilage Proteoglycan ◽  
Flavobacterium Heparinum

scholarly journals Role of arginine 292 in the catalytic activity of chondroitin AC lyase from Flavobacterium heparinum

2002 ◽  
Vol 1597 (2) ◽  
pp. 260-270 ◽  
Author(s):  
Ishan Capila ◽  
Yi Wu ◽  
David W Rethwisch ◽  
Allan Matte ◽  
Miroslaw Cygler ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Chondroitin Ac Lyase ◽  
Flavobacterium Heparinum

scholarly journals Expression System for High Levels of GAG Lyase Gene Expression and Study of the hepA Upstream Region in Flavobacterium heparinum

2002 ◽  
Vol 184 (12) ◽  
pp. 3242-3252 ◽  
Author(s):  
Françoise Blain ◽  
A. Lydia Tkalec ◽  
Zhongqi Shao ◽  
Catherine Poulin ◽  
Marc Pedneault ◽  
...  
Keyword(s):  
Transcriptional Start Site ◽  
Expression System ◽  
Regulatory Region ◽  
Start Codon ◽  
Upstream Region ◽  
Wild Type ◽  
Heparinase I ◽  
High Level ◽  
Flavobacterium Heparinum ◽  
Transcriptional Start Sites

ABSTRACT A system for high-level expression of heparinase I, heparinase II, heparinase III, chondroitinase AC, and chondroitinase B in Flavobacterium heparinum is described. hepA, along with its regulatory region, as well as hepB, hepC, cslA, and cslB, cloned downstream of the hepA regulatory region, was integrated in the chromosome to yield stable transconjugant strains. The level of heparinase I and II expression from the transconjugant strains was approximately fivefold higher, while heparinase III expression was 10-fold higher than in wild-type F. heparinum grown in heparin-only medium. The chondroitinase AC and B transconjugant strains, grown in heparin-only medium, yielded 20- and 13-fold increases, respectively, in chondroitinase AC and B expression, compared to wild-type F. heparinum grown in chondroitin sulfate A-only medium. The hepA upstream region was also studied using cslA as a reporter gene, and the transcriptional start site was determined to be 26 bp upstream of the start codon in the chondroitinase AC transconjugant strain. The transcriptional start sites were determined for hepA in both the wild-type F. heparinum and heparinase I transconjugant strains and were shown to be the same as in the chondroitinase AC transconjugant strain. The five GAG lyases were purified from these transconjugant strains and shown to be identical to their wild-type counterparts.

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