Enzymic degradation of heparin. A sulphamidase and a sulphoesterase from Flavobacterium heparinum.
A sulphamidase and a sulphoesterase were isolated from adapted cells of Flavobacterium heparinum. These enzymes were partially purified from the ;heparinases' present in the bacterial extracts and characterized. The sulphamidase has a high specificity for glucosamine N-sulphate and glucosamine 2,6-disulphate. The activity decreases sharply with increasing molecular weight of the substrates tested. The sulphamidase and the sulphoesterase activities were distinguished from each other by their different sensitivities to concentration of phosphate ion and to temperature. The importance of these enzymes in the study of the structure of heparin is discussed.
D005417:Flavobacterium / Q000201:enzymology*; D005944:Glucosamine / Q000378:metabolism; D006493:Heparin / Q000378:metabolism*; D008970:Molecular Weight; D010710:Phosphates; D013429:Sulfatases / Q000032:analysis*; D013431:Sulfates / Q000378:metabolism; D013696:Temperature; D014461:Ultracentrifugation; D014465:Ultrasonics
D010710:Phosphates; D013431:Sulfates; D006493:Heparin; D013429:Sulfatases; D005944:Glucosamine