Kevin Schey
Last active: 3/24/2020

Purification and characterization of lysozyme from plasma of the eastern oyster (Crassostrea virginica).

Xue QG, Schey KL, Volety AK, Chu FL, La Peyre JF
Comp Biochem Physiol B Biochem Mol Biol. 2004 139 (1): 11-25

PMID: 15364284 · DOI:10.1016/j.cbpc.2004.05.011

Lysozyme was purified from the plasma of eastern oysters (Crassostrea virginica) using a combination of ion exchange and gel filtration chromatographies. The molecular mass of purified lysozyme was estimated at 18.4 kDa by SDS-PAGE, and its isoelectric point was greater than 10. Mass spectrometric analysis of the purified enzyme revealed a high-sequence homology with i-type lysozymes. No similarity was found however between the N-terminal sequence of oyster plasma lysozyme and N-terminal sequences of other i-type lysozymes, suggesting that the N-terminal sequences of the i-type lysozymes may vary to a greater extent between species than reported in earlier studies. The optimal ionic strength, pH, cation concentrations, sea salt concentrations, and temperature for activity of the purified lysozyme were determined, as well as its temperature and pH stability. Purified oyster plasma lysozyme inhibited the growth of Gram-positive bacteria (e.g., Lactococcus garvieae, Enterococcus sp.) and Gram-negative bacteria (e.g., Escherichia coli, Vibrio vulnificus). This is a first report of a lysozyme purified from an oyster species and from the plasma of a bivalve mollusc.

MeSH Terms (20)

Amino Acid Sequence Animals Anti-Bacterial Agents Cations Electrophoresis, Polyacrylamide Gel Enzyme Stability Hemolymph Hydrogen-Ion Concentration Isoelectric Point Louisiana Molecular Sequence Data Molecular Weight Muramidase Osmolar Concentration Ostreidae Seawater Sequence Alignment Sequence Analysis, Protein Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Temperature

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