{"refrec":{"BRefID":10652,"RR":"<b>Jebsen, J.W.</b> (1962). Proteins in fish muscle, <b><i>in</i></b>: Heen, E. <i>et al.</i> <i>Fish in nutrition.</i> pp. 68-72","BEntID":10652,"PublicFlag":1,"CheckedFlag":0,"wosflag":null,"vabbflag":null,"RefStringPartII":", <b><i>in</i></b>: Heen, E. <i>et al.</i> <i>Fish in nutrition.</i> pp. 68-72","DocTypID":17,"DocType":"Book chapters","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Jebsen, J.W.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Jebsen, J.W.","Englishabstract":"(1) The proteins of muscle fibrines, tropomyosin, actin, myosin and actomyosin: 65 per cent of fish muscle protein (40% in mammals). (2) The proteins of cytoplasma (enzymes in muscle metabolism), globulin x, myogen, myoglobin: 26-30 % of fish muscle protein (35-40 per cent in mammals). (3) The proteins of the connective tissue, stromaproteins (collagen): 3 % of the muscle of teleost; 10% in elasmobranch (17 per cent in mammals). Group 1: extractable with neutral salt solution of high ionic strength >= 0.5. Group 2: extractable with neutral salt solution of low ionic strength <= 0.15.  Group 3: not extractable with neutral salt solution, nor in diluted acids and alkalies. Group 1 has great crystal lattice energy and great dipole moment; this results in great sensitivity towards salt ionesGroup 2 is rich in charged side chains, but has a small dipole moment; this results in a lower sensitivity towards salt iones. Precipitation of fish proteins: percentage saturation of ammonium sulphate. Tropomyosin: 50-66 Myosin: 35-48Actin: 10-20Actomyosin: 28-38 Result of electrophoresis:Both pure actomyosin and pure actin give one sharp peak. Pure myosin gives a broader peak; this may indicate some heterogeneity. Myogen gives 7 components by Tiselius-electrophoresis. Each species of fishes gives a different pattern. Electrophoresis in starchgel gives 12 components at pH 7.5.Results by ultracentrifuge:Both actomyosin and tropomyosin give one sharp peak. Myosin is not homogeneous. Myogen gives four componements.Crystallized fish protein:Myogen proteins, myoglobin and tropomyosin. In the white muscle, glycogenic metabolism predominates; in the red muscle <i>(Musculus lateralis superficialis trunci)</i> the citric acid cycle probably prevails. The red muscle (e.g. in tuna) seems to be a passive muscle with a high oxygen metabolism. The white muscle is an active muscle with low oxygen supply.","AbstractOtherLang":"Protéines dans le muscle du poisson(1) Protéines des fibrilles musculaires, tropomyosine, actine, myosine et actomyosine: 65% des protéines du muscle de poisson (40% chez les mammifères). (2) Protéines du cytoplasme (enzymes dans le métabolisme musculaire), globuline x, myogène, myoglobine: 26-30% des protéines du muscle de poisson (35-40% chez les mammifères). (3) Protéines du tissu conjonctif, stromaprotéines (collagène): 3% du muscle de téléostéen; 10% chez les élasmobranches; (17% chez les mammifères). Groupe 1: extractible avec une solution de sel neutre de haute force ionique >= 0,5.  Groupe 2: extractible avec une solution de sel neutre de faible force ionique <=0,15.   Groupe 3: non extractible avec une solution de sel neutre, ni dans les acides dilués et les alcalis. Le Groupe 1 est d'une grande énergie de réseau cristallin et d'un grand moment dipolaire; ceci se traduit par une grande sensibilité à l'égard des ions salins. Le Groupe 2 est riche en chaines à charges latérales, mais d'un faible moment dipolaire; ceci se traduit par une moindre sensibilité à l'égard des ions salins. Précipitation des protéines du poisson: pourcentage de la saturation en sulfate d'ammonium.Tropomyosine: 50-66 Myosine: 35-48Actine:10-20Actomyosine: 28-38 Résultats de l'électrophorèse:L'actomyosine pure et l'actine pure donnent toutes deux un sommet aigu. La myosine pure donne un sommet élargi qui peut indiquer la présence de quelque heterogenéité. Le myogene donne 7 constituants par l'électrophorèse de Tiselius. Chaque espèce de poissons donne une disposition différente. L'électrophorèse dans le gel d'empois d'amidon donne 12 constituants au pH 7,5. Résultats de l'ultra-centrifugation: L 'actomyosine et la tropomyosine donnent toutes deux un sommet aigu. La myosine n'est pas homogène. Le myogène donne quatre constituants. Protéines cristallisées du poisson: Protéines du myogene, myoglobine et tropomyosine. Dans le muscle blanc, le métabolisme glycogénique prédomine; dans le muscle rouge <i>(Musculus lateralis superficialis trunci)</i> c'est probablement le cycle de l'acide citrique qui prévaut. Le muscle rouge (par exemple chez le thon) semble être un muscle passif avec un haut métabolisme de l'oxygène. Le muscle blanc est un muscle actif avec un faible apport d'oxygène.","BibLvlCode":"AM","StandardTitle":"Proteins in fish muscle","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":1962,"MonPub":null,"DateUpdate":"2001-11-14","DateCreate":"2001-06-06","SecASFANote":null,"ConfID":null,"PeerRev":null,"VlizCoreFlag":1,"WoScode":null,"VABBcode":null,"OpenAcc":0},"refs":null,"anarec":{"AnaID":10652,"PubliDate":1962,"Pagination":"68-72","XtraPublOfAnaID":null,"ISBN":null,"Volume":null,"Issue":null,"BRefMon":10616,"BRefMonRR":"<b>Heen, E.; Kreuzer, R.</b> (1962). Fish in nutrition. Fishing News (Books): London. XXIII, 447 pp.","BRefXtra":null,"BRefXtraRR":null,"SerBRefID":null,"SerRR":null,"StandardTitleSer":null,"ISSN":null,"AbbrevSer":null,"StandardTitleMon":"Fish in nutrition","StartPage":68,"Pages":5,"ToPubliDate":null,"BRefBibLvlCode":"M","SerNotes":null,"AutString":"Heen, E.; Kreuzer, R."},"monrec":null,"serrec":null,"relations":null,"relationsRev":null,"addrec":null,"othpubs":null,"ownerships":null,"authors":[{"AutName":"Jebsen","Firstname":"Jens","Initials":"J.W.","Affiliation":null,"Discriminator":null,"CorporateFlag":0,"BEntID":10652,"AutID":14945,"OrderNr":1,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":null,"InsFSN":null,"ORCID":null,"PersID":null,"InsID":null}],"mapdetails":null,"datasets":null,"monographs":null,"monparts":null,"serparts":null,"BEntOpen":null,"BEntPrivate":null,"availability":null,"litstyles":null,"thespers":null,"arch2discl":null,"SERpubls":null,"MONpubls":[{"PublName":"Fishing News (Books)","Place":"London"}],"pictures":[],"thestermsPath":null,"thestermsASFA":null,"taxtermsASFA":null,"geotermsASFA":null,"collections":null,"conf":null,"proj":null,"Physdatasets":null,"spcols":null,"doi":null,"publs":null,"serparttypes":null,"monauthors":[{"AutName":"Heen","Initials":"E.","CorporateFlag":0,"BEntID":10616,"AutID":14884,"OrderNr":1,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"AutStrTrunc":"Heen, E.; Kreuzer, R."},{"AutName":"Kreuzer","Initials":"R.","CorporateFlag":0,"BEntID":10616,"AutID":14885,"OrderNr":2,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"AutStrTrunc":"Heen, E.; Kreuzer, R."}],"MParts":null,"SParts":null,"hLibs":null,"langs":[{"BEntID":10652,"AbstractFlag":0,"LangID":15,"LangCode":"en","Lang":"English","DutchTerm":"Engels","LangCodeExtended":"eng"},{"BEntID":10652,"AbstractFlag":0,"LangID":22,"LangCode":"fr","Lang":"French","DutchTerm":"Frans","LangCodeExtended":"fre"},{"BEntID":10652,"AbstractFlag":1,"LangID":22,"LangCode":"fr","Lang":"French","DutchTerm":"Frans","LangCodeExtended":"fre"}],"urls":null,"thesterms":null,"taxterms":null,"geoterms":null,"othterms":null,"asfacodes":null,"asfa2codes":null,"thestermsFRIS":null,"taxtermsFRIS":null,"geotermsFRIS":null,"othtermsFRIS":null,"resmessage":"","complete":1,"sessions":{"newSesName":"VLIZ2000\\stevenc","newSesDate":{"date":"2001-06-06 08:06:32.307000","timezone_type":3,"timezone":"Europe/Brussels"},"updSesName":"Haspeslagh, Jan, J.","updSesDate":{"date":"2001-11-14 11:50:31.853000","timezone_type":3,"timezone":"Europe/Brussels"}}}
