These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification and partial characterization of an acid proteinase from Dirofilaria immitis.
    Author: Sato K, Nagai Y, Suzuki M.
    Journal: Mol Biochem Parasitol; 1993 Apr; 58(2):293-9. PubMed ID: 8479453.
    Abstract:
    An acid proteinase of Dirofilaria immitis worms was purified 437-fold by gel filtration on Sephadex G-75 followed by pepstatin-agarose gel affinity chromatography. The enzyme with a molecular weight of 42,000 and specific activity of 384 units (mg protein)-1 was homogeneous as judged by both affinity chromatography and SDS-polyacrylamide gel electrophoresis. However, polyacrylamide disc electrophoresis at pH 8.9 revealed that the enzyme is composed of 5 multiforms, all carrying proteinase activity. Optimum pH of the enzyme was in the range of pH 2.8-3.4, and its isoelectric point ranged between 5.8 and 6.4. The purified proteinase showed a potent activity against hemoglobin and myoglobin releasing acid soluble peptides, but not free amino acids. Complete inhibition of the proteolytic activity by pepstatin in the order of 10(-7) M strongly suggests that the enzyme belongs to the carboxyl-proteinase family.
    [Abstract] [Full Text] [Related] [New Search]