{"refrec":{"BRefID":297274,"RR":"<b>Myrnes, B.; Seppola, M.; Johansen, A.; Øverbø, K.; Callewaert, L.; Vanderkelen, L.; Michiels, C.W.; Nilsen, I.W.</b> (2013). Enzyme characterisation and gene expression profiling of Atlantic salmon chicken- and goose-type lysozymes. <i>Dev. Comp. Immunol. 40(1)</i>: 11-19. <a href=\"https://dx.doi.org/10.1016/j.dci.2013.01.010\" target=\"_blank\">https://dx.doi.org/10.1016/j.dci.2013.01.010</a>","BEntID":289363,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Dev. Comp. Immunol. 40(1)</i>: 11-19. <a href=\"https://dx.doi.org/10.1016/j.dci.2013.01.010\" target=\"_blank\">https://dx.doi.org/10.1016/j.dci.2013.01.010</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Myrnes, B.; Seppola, M.; Johansen, A.; Øverbø, K.; Callewaert, L.; Vanderkelen, L.; Michiels, C.W.; Nilsen, I.W.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Myrnes, B. <i>et al.</i>","Englishabstract":"Lysozymes represent important innate immune components against bacteria. In this study, Atlantic salmon (<i>Salmo salar</i>) goose (g-) and chicken (c-) types of lysozyme were subjected to protein characterisations and tissue expression analyses. Specific bacterial protein inhibitors of g- and c-type lysozymes were employed to discriminate between respective enzyme activities. Blood, gills and liver contained activities exclusive for the g-type lysozyme. Only haematopoietic organs (head kidney and spleen) contained enzyme activities of both g- and c-lysozyme enzymes and c-type activity was not found outside these organs. Gene transcript levels proportional to enzyme activity levels were detected for the g-type lysozyme but not for the c-type. <i>In vitro</i> studies revealed significant induction of c-type gene expression and enzyme activity in macrophages after incubation with lipopolysaccharide (LPS) while expression of the g-type lysozyme gene was unaffected. The activity of purified native c-type enzyme was profoundly reduced by divalent cations and displayed low tolerance to monovalent cations, while the native g-type lysozyme was stimulated by monovalent cations and tolerated low concentrations of divalent cations. Activities of both enzymes increased with temperature elevations up to 60 °C. The native g-type lysozyme responses to temperature in particular are in apparent conflict to the ones for the recombinant salmon g-lysozyme.Our results imply separate expression regulations and different functions of c- and g-type lysozymes in salmon. LPS-induced expression of c-type lysozyme and broad constitutive tissue distribution of g-type lysozyme in salmon is different from findings in other studied fish species.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Enzyme characterisation and gene expression profiling of Atlantic salmon chicken- and goose-type lysozymes","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-21 01:32:41.752876","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Lysozyme, Purification, Activity, Gene expression, Ivy, PliG","OtherDescriptors":null,"Notes":null,"AnaPub":2013,"MonPub":null,"DateUpdate":"2022-05-18","DateCreate":"2018-07-02","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000317874200002","VABBcode":"vabb:384265","OpenAcc":0,"DOI":"10.1016/j.dci.2013.01.010"},"refs":null,"anarec":{"AnaID":297274,"PubliDate":2013,"Pagination":"11-19","XtraPublOfAnaID":null,"ISBN":null,"Volume":"40","Issue":"1","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":120980,"SerRR":"Developmental and Comparative Immunology. 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