1887

Abstract

The culture supernatant of promoted the disruption of human red blood cells (RBCs). The haemolytic activity was detected in a sugar-rich fraction (about 200 kDa) from Sephacryl S-100 chromatography. As the haemolytic activity was adsorbed by concanavalin A-Sepharose, the haemolytic factor may be a mannoprotein. The activity was inactivated by periodate oxidation, indicating that the sugar moiety of the mannoprotein played an important role in the haemolysis. The structure of the sugar moiety of the mannoprotein was identified as a cell-wall mannan by H-NMR analysis, and purified mannan promoted the disruption of RBCs. The binding of mannan to RBCs was demonstrated by flow cytometric analysis and was inhibited by the addition of band 3 protein inhibitor, 4,4′-diisothio-cyanatostilbene-2,2′-disulfonic acid (DIDS). The haemolysis caused by mannan was inhibited by DIDS, SITS (4-acetamido-4′-isothiocyanatostilbene-2,2′-disulfonic acid) and bis(sulfosuccinimidyl) suberate, but not by pyridoxal 5-phosphate. These results indicated that a mannoprotein released from bound to the band 3 protein on RBCs, thereby promoting their disruption.

Loading

Article metrics loading...

/content/journal/micro/10.1099/13500872-145-3-689
1999-03-01
2019-10-15
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/13500872-145-3-689
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error