Ontology highlight
ABSTRACT:
SUBMITTER: Hanada Y
PROVIDER: S-EPMC3234760 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
The Journal of biological chemistry 20110920 45
Silkworm hemolymph inhibits hemolysin production by Staphylococcus aureus. We purified a factor in the silkworm hemolymph responsible for this inhibitory activity. The final fraction with the greatest specific activity contained 220- and 74-kDa proteins. Determination of the N-terminal amino acid sequence revealed that the 220- and 74-kDa proteins were apolipophorin I and apolipophorin II, respectively, indicating that the factor was apolipophorin (ApoLp). The purified ApoLp fraction showed decr ...[more]