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. 1969 Jan;111(1):91–95. doi: 10.1042/bj1110091

Enzymic degradation of heparin A sulphamidase and a sulphoesterase from Flavobacterium heparinum

Carl P Dietrich 1
PMCID: PMC1187498  PMID: 5775690

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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