@article{oai:oacis.repo.nii.ac.jp:00002554,
 author = {Kondo, Hidehiro and Murotani, Fuyuka and Koiwai, Keiichiro and Hirono, Ikuo},
 journal = {Developmental & Comparative Immunology},
 month = {Sep},
 note = {We examined lysozyme activities in the serum and the leukocyte extracts of the banded houndshark Triakis scyllium.
The serum exhibited lytic activity, but not the leukocyte extracts.
The lytic substance in the serum was of approximately 14 kDa and the N-terminal amino acid sequence was YVYSK.
cDNA cloning identified a C-type lysozyme (TsLysC) gene and two G-type lysozyme (TsLysG) cDNA clones of different lengths.
The TsLysC gene encodes 149 amino acids residues, and the sequence derived from the N-terminal amino acid sequencing was displayed at position 17–21. TsLysG, on the other hand, contains two ORFs that are homologous to the N- and C-terminal regions of G-type lysozyme of other fish species.
TsLysC mRNA levels were high in the liver. TsLysG mRNA level was significantly lower than TsLysC mRNA in the liver., 公開日: 2023-06-04, 18H03958},
 title = {Chicken-type lysozyme is a major bacteriolytic enzyme in the blood of the banded houndshark Triakis scyllium},
 volume = {134},
 year = {2022}
}