Iw. Nilsen et al., Protein purification and gene isolation of chlamysin, a cold-active lysozyme-like enzyme with antibacterial activity, FEBS LETTER, 464(3), 1999, pp. 153-158
An antibacterial similar to 11 kDa protein designated chlamysin was isolate
d from viscera of the marine bivalve Chlamys islandica. Chlamysin inhibited
the growth of ail Grampositive and Gram-negative bacteria tested. The isol
ated protein was highly efficient in hydrolyzing Micrococcus luteus cells o
nly at low pH (4.5-6.2) and at low temperature (4-35 degrees C), No signifi
cant loss of enzyme activity was observed after 30 days storage at room tem
perature or after heating to 70 degrees C for 15 min, suggesting relatively
high protein structure stability. Sequence-analyzed fragments of the prote
in revealed data which guided the isolation of the cDNA gene, encoding a 13
7 amino acid chlamysin precursor in scallops. The deduced protein contains
a high portion of cysteine, serine and histidine residues and has a predict
ed isoelectric point below 7, The chlamysin protein was found to have seque
nce homology to an isopeptidase and to a recently published bivalve lysozym
e, (C) 1999 Federation of European Biochemical Societies.