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At least 523 records · Page 29Linked to original sources
PubMed2005

Gene cloning and functional analysis of glycosaminoglycan-degrading enzyme chondroitin AC lyase from Flavobacterium columnare G4.

The chondroitin AC lyase gene, cslA, was cloned for the first time from the fish bacterial pathogen F. columnare G4. From the first transcription initiation site, the cslA extends 2620 nucleotides to the end of the 3' region. The open reading frame of cslA transcript has 2286 nucleotides encoding 762 amino acids with a 16 residues long signal peptide at the N-terminus. The gene, cslA was then successfully expressed in Escherichia coli and recombinant chondroitin AC lyase, rChonAC was purified, with its lytic activity analyzed. Zymography analysis copolymerized with chondroitin sulphate revealed the lytic activity of rChonAC and also the crude native ChonAC isolated from periplamic space of cultured F. columnare G4. The low level of lytic activity observed in crude native ChonAC may be due possibly to the low level of expression of this gene in the cultured condition. The expression and the role of this virulence factor is of interest for further research on the pathogenesis of F. columnare.

Amino Acid Sequence↗
PubMed1980

A novel purification procedure of L-lysine 6-aminotransferase from Flavobacterium lutescence.

A new method for the purification of L-lysine 6-aminotransferase (L-lysine: 2-oxoglutarate 6-aminotransferase, EC 2.6.1.36) was devised, in which affinity chromatography with L-lysylacetamidododecyl-Sepharose 6B, the most effective affinity adsorbent, was substituted for the heat treatment. The yield of the enzyme with the present procedure was approx. twice as high as that with the previous procedure (Soda, K. and Misono, H. (1968) Biochemistry 7, 4110-4119). The enzyme purified by this method was activated 2-fold by heat treatment (65 degrees C for 5 min). The enzyme has absorption maxima at 340 and 415 nm, derived from the bound pyridoxal 5'-phosphate, which are identical with those of the enzyme obtained with the procedure including heat treatment. These results rule out the possibility that the formation of the 340-nm pyridoxal 5'-phosphate of the enzyme is an artifact of heat treatment.

Chromatography, Affinity↗
PubMed2006

Effect of CaCl2 as activity stabilizer on purification of heparinase I from Flavobacterium heparinum.

Heparinase I has been purified from F. heparinum by a novel scheme with 10mM CaCl(2) added in crude extracts of cells. The enzyme was purified to apparent homogeneity through ammonium sulfate precipitation, Octyl-Sepharose chromatography, CM-52 chromatography, SP-650 chromatography, and Sephadex G-100 gel filtration chromatography. The specific activity of the purified enzyme was 90.33 U/mg protein with a purification fold of 185.1. The yield was 17.8%, which is higher than any previous scheme achieved. The molecular weight of the purified enzyme was 43 kDa with a pI of 8.5. It has an activity maximum at pH range of 6.4-7.0 and 41 degrees C. CaCl(2) is a good stabilizer of the purified enzyme in liquid form toward either storaging at 4 degrees C or freezing-thawing.

Calcium Chloride↗