{"refrec":{"BRefID":10660,"RR":"<b>Hamoir, G.</b> (1962). The amino acid composition of fish muscle proteins, <b><i>in</i></b>: Heen, E. <i>et al.</i> <i>Fish in nutrition.</i> pp. 73-75","BEntID":10660,"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. 73-75","DocTypID":17,"DocType":"Book chapters","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Hamoir, G.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Hamoir, G.","Englishabstract":"Present evidence points to the existence of a fundamental amino-acid plan for the constitution of the proteins of the myofibril: myosin, actin and tropomyosin, of the lower as well as the higher vertebrates. The opposite, however, occurs in the case of the proteins dissolved in the sarcoplasm (myogen). The electrophoretic patterns of the myogens of fish are characteristic of each species; they differ from those of warm-blooded vertebrates by a common higher average mobility. On the other hand, the myogens of fish contain proteins having rates of sedimentation of 1.3-1.5, 4.5-5.0 and 6.5-7.2 S. The first group is absent in the case of warm-blooded vertebrates myogens. It amounts to as much as about 50 per cent in carp myogen. When isolated and subjected to electrophoresis at neutral pH, this fraction resolves in the case of the carp into three peaks. Two components migrating at the levels of the second and third peaks have been isolated. The study of their properties has shown that their molecular weight is around 14,000, and their amino-acid compositions extremely abnormal. A major component, having a rate of sedirnentation of 5 S and a high electrophoretic mobility, has also been isolated from carp myogen. A corresponding component does not seem to exist in warm-blooded vertebrates. lnvestigations carried out on carp aldolase and carp glyceraldehyde deshydrogenase have shown that their electrophoretic mobilities are low at ph 7, and sirnilar to (if not identical with) those of the corresponding rabbit muscle enzymes. These results suggest that, as against the myogen of warm-blooded animals which is usually assumed to be made up mainly of glycolytic enzymes, the myogen of cold-blooded vertebrates contains three distinct groups of proteins: the first one, not observed in the case of other vertebrates and containing proteins of small molecular weight and very unusual amino-acid composition; a second one, with a sedimentation rate of 5 S and a fairly high electrophoretic mobility; and a third one corresponding to glycolytic enzymes. Some components of the fish myogen may form a protein reserve, or may have some biological function not occurring in warm-blooded muscle which has still to be defined.","AbstractOtherLang":"La composition en amino-acides des protéines du muscle de poisson:Les protéines intervenant dans la composition des myofibrilles (myosine, actine, tropomyosine) ont la même composition en acides aminés dans le cas de tous les vertébrés. Par contre, les protéines du sarcoplasme formant le myogene different à ce point de vue suivant leur origine. Les diagrammes électrophorétiques de myogènes de vertébrés à sang-froid different d'une espèce à l'autre, et se distinguent de ceux vertébrés à sang-chaud par une mobilité moyenne plus élevée. Les myogènes de poissons se scindent à l'ultracentrifugation en trois groupes de protéines de vitesses de sédimentation 1,3-1,5, 4,5-5,0, et 6,5-7,2 S. Le premier groupe n'existe pas dans les myogènes des vertébrés à sang-chaud. Il représente chez la carpe environ 50% du myogène. Lorsqu'on l'isole de muscles de carpe et l'analyse par électrophorèse à pH neutre, il se scinde en trois gradients. Des composants migrant au niveau du deuxième et du troisième gradient ont été isolés. L'étude de leurs propriétés ont montré que leurs poids moléculaires est d'environ 14.000 et que leurs compositions en acides aminés sont extrêmement anormales. Un composant important de vitesse 5 S et de mobilité électrophorétique élevée a aussi été isolé du myogène de carpe. Il ne parait pas représenté dans le myogène des vertébrés supérieurs. Des recherches relatives à l'aldolase de carpe et à la glycéraldéhyde déshydrogénase de carpe ont montré que leurs mobilités électrophorétiques sont peu élevées à pH 7, et semblables (sinon identiques) à celles des enzymes musculaires correspondants du lapin. Ces résultats suggerent que le myogène de poisson contient trois groupes de protéines: le premier, qu'on n'observe pas chez les autres vertébrés et qui contient des protéines de poids moléculaire très faible et de compositions en acides aminés tres anormales; le deuxième, de vitesse de sédimentation de 5 S et de mobilité électrophorétique élevée ; et le troisième correspondant aux enzymes glycolytiques. II est possible que certains constituants du myogène de poisson forment une réserve protéique ou assurent une fonction biologique n'existant pas dans le cas des vertébrés supérieurs qui reste encore à identifier .","BibLvlCode":"AM","StandardTitle":"The amino acid composition of fish muscle proteins","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":"2001-06-06","DateCreate":"2001-06-06","SecASFANote":null,"ConfID":null,"PeerRev":null,"VlizCoreFlag":1,"WoScode":null,"VABBcode":null,"OpenAcc":0},"refs":null,"anarec":{"AnaID":10660,"PubliDate":1962,"Pagination":"73-75","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":73,"Pages":3,"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":"Hamoir","Firstname":"Gabriel","Initials":"G.","Affiliation":null,"Discriminator":null,"CorporateFlag":0,"BEntID":10660,"AutID":8140,"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":10660,"AbstractFlag":0,"LangID":15,"LangCode":"en","Lang":"English","DutchTerm":"Engels","LangCodeExtended":"eng"},{"BEntID":10660,"AbstractFlag":0,"LangID":22,"LangCode":"fr","Lang":"French","DutchTerm":"Frans","LangCodeExtended":"fre"},{"BEntID":10660,"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":"VLIZ2000\\stevenc","updSesDate":{"date":"2001-06-06 08:06:32.307000","timezone_type":3,"timezone":"Europe/Brussels"}}}