{"refrec":{"BRefID":217728,"RR":"<b>Huriaux, F.; Vandewalle, P.; Baras, E.; Legendre, M.; Focant, B.</b> (1999). Myofibrillar proteins in white muscle of the developing African catfish <i>Heterobranchus longifilis</i> (Siluriforms, Clariidae). <i>Fish Physiol. Biochem. 21(4)</i>: 287-301. <a href=\"http://dx.doi.org/10.1023/A:1007835101472\" target=\"_blank\">http://dx.doi.org/10.1023/A:1007835101472</a>","BEntID":209473,"PublicFlag":1,"CheckedFlag":0,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>Fish Physiol. Biochem. 21(4)</i>: 287-301. <a href=\"http://dx.doi.org/10.1023/A:1007835101472\" target=\"_blank\">http://dx.doi.org/10.1023/A:1007835101472</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":1,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Huriaux, F.; Vandewalle, P.; Baras, E.; Legendre, M.; Focant, B.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Huriaux, F. <i>et al.</i>","Englishabstract":"Developmental changes in myofibrillar protein composition were investigated in the myotomal muscle of the African catfish, <i>Heterobranchus longifilis</i> (Clariidae), by several electrophoretic techniques. The main muscle fibres of larvae and the fast-white muscle fibres of juvenile and adult fish were found to express distinct myosin heavy chain and myosin light chain 2 (LC2) isoforms. Three myosin LC2 chains were successively detected, differing by their isoelectric points. In contrast, the alkali light chains remained qualitatively and quantitatively unchanged during fish growth. Actin, <img src=\"/content/K40252T001043276/xxlarge945.gif\" alt=\"agr\" align=\"BASELINE\" border=\"0\">-tropomyosin, and troponin-C (TN-C) were also similar in larval, juvenile, and adult white muscle, but an additional larval tropomyosin isoform was found in the first developmental stages. Two isoforms of troponin-T (TN-T) and troponin-I (TN-I) were synthesised in the course of fish growth. Transition from the larval to the adult isoform was much faster for TN-T than for TN-I. Slow-red muscle myofibrils from adult <i>H. longifilis</i> showed no common component (except actin) with larval, juvenile, or adult fast-white muscle myofibrils. Red myofibrils displayed a single TN-T and a single TN-I isoform, but two isoforms of TN-C. The myofibrillar protein isoforms synthesised at any given developmental stage almost certainly reflect changes in the functional requirements of swimming muscles in the course of fish development.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Myofibrillar proteins in white muscle of the developing African catfish <i>Heterobranchus longifilis</i> (Siluriforms, Clariidae)","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-19 01:31:32.310745","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"development; fish; myosin heavy chain; myosin light chain; polyacrylamide gel electrophoresis; tropomyosin; troponin-C; troponin-I; troponin-T","OtherDescriptors":null,"Notes":null,"AnaPub":1999,"MonPub":null,"DateUpdate":"2015-11-04","DateCreate":"2012-08-28","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000085987500001","VABBcode":null,"OpenAcc":0,"DOI":"10.1023/A:1007835101472"},"refs":null,"anarec":{"AnaID":217728,"PubliDate":1999,"Pagination":"287-301","XtraPublOfAnaID":null,"ISBN":null,"Volume":"21","Issue":"4","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42694,"SerRR":"Fish Physiology and Biochemistry. Springer: Dordrecht.  ISSN 0920-1742; e-ISSN 1573-5168","StandardTitleSer":"Fish Physiology and Biochemistry","ISSN":"0920-1742","AbbrevSer":"Fish Physiol. 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