1. 1. This study was undertaken to partially purify the hemolysin from the coelomic fluid of Strongylocentrotus nudus by a combination of affinity, hydrophobic and gel filtration chromatographies, and to investigate the property of this molecule. 2. 2. The hemolysin was purified about 120-fold by gel filtration and the chromatographic behavior indicated that the intact molecule of the hemolysin had a molecular mass of 200 kDa. 3. 3. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, under non-reducing condition, a single band of 40 kDa protein disappeared with absorption by rabbit and sheep erythrocytes. 4. 4. It was suggested that this hemolysin molecule, with a single subunit of 40 kDa, had a physiological function as an opsonin.
|Number of pages||7|
|Journal||Comparative Biochemistry and Physiology -- Part B: Biochemistry and|
|Publication status||Published - 1993 May|
ASJC Scopus subject areas
- Molecular Biology