Partial purification and characterization of hemolysin from the coelomic fluid of Strongylocentrotus nudus

Makoto Osada, Toshimitsu Ito, Takeshige Matsutani, Katsuyoshi Mori

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)43-49
Number of pages7
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume105
Issue number1
DOIs
Publication statusPublished - 1993 May

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology

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