Enzymic degradation of heparin A sulphamidase and a sulphoesterase fromFlavobacterium 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.
In order to observe the efficacy of the towel finished by the sanitary finishing agent containing quaternary ammonium salt in destruction of HBsAg, carrier test and ELISA method were used for examination. Results: The HBsAg contaminating the surface of the towel finished by the sanitary finishing agent containing quaternary ammonium salt 1000 mg/L could be converted to negative after exposure for 8 h at 20℃. The results indicate that the sanitary finishing agent on the towel has destructive effect on HBsAg.