Barbus; Fish; Parvalbumins; Heavy chains; Light chains; Myosin
Abstract :
[en] Muscle proteins were investigated in two large European barbels, Barbus barbus and B. meridionalis, and in four small tropical barbels native to SE Asia: B. conchonius, B. tetrazona, B. sachsi and B. titteya. Polyacrylamide gel electrophoresis was used to analyse myosin heavy and light chains and parvalbumin isotypes from white trunk muscle. Each species could be biochemically identified. The myosin subunit and parvalbumin isotype patterns obtained for the two European barbels were similar. The Asian barbels, on the other hand, not only differed from the European species but displayed a greater diversity within their group. These biochemical results are largely in agreement with morphological and genetic data, but fail to substantiate suggested close relationships between Asian barbel species.
Disciplines :
Aquatic sciences & oceanology
Author, co-author :
Huriaux, Françoise ; Laboratoire de Biologie cellulaire et tissulaire, Université de Liège, rue de Pitteurs, 20, Liège, B-4020, Belgium
Vandewalle, Pierre ; Université de Liège - ULiège > Département de Biologie, Ecologie et Evolution > Département de Biologie, Ecologie et Evolution
Focant, Bruno ; Laboratoire de Biologie cellulaire et tissulaire, Université de Liège, rue de Pitteurs, 20, Liège, B-4020, Belgium
Language :
English
Title :
Polymorphism of white muscle myosin and parvalbumins in the genus Barbus (Teleostei: Cyprinidae)
Publication date :
December 1992
Journal title :
Journal of Fish Biology
ISSN :
0022-1112
eISSN :
1095-8649
Publisher :
Blackwell, Oxford, United Kingdom
Volume :
41
Issue :
6
Pages :
873-882
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
FRSM - Fonds de la Recherche Scientifique Médicale F.R.S.-FNRS - Fonds de la Recherche Scientifique
scite shows how a scientific paper has been cited by providing the context of the citation, a classification describing whether it supports, mentions, or contrasts the cited claim, and a label indicating in which section the citation was made.
Bibliography
Almaça C. (1984) Form relationships among western Palearctic species of Barbus (Cyprinidae, Pisces). Arquivos do Museu Bocage 2:207-248.
Berrebi P., Le Brun N., Renaud F., Lambert A. (1987) Hybridation inter‐spécifique de deux Cyprinidae (genre Barbus). Conséquence sur la spécificité parasitaire de D. gracile (Monogenea). Actes du Colloque National du C.N.R.S. ‘Biologic des Populations’, I.A.S.B.S.E., C. Bernard, Lyon; .
Berrebi P., Lévêque C., Cattaneo‐Berrebi G., Agnèse J.F., Guégan J.F., Machordom A. (1990) Diploid and tetraploid African Barbus (Osteichthyes, Cyprinidae): on the coding of differential gene expression. Aquatic Living Resources 3:313-323.
Danieli Betto D., Zerbato E., Betto R. (1986) Type 1, 2A, and 2B myosin heavy chain electrophoretic analysis of rat muscle fibers. Biochemical and Biophysical Research Communications 138:981-987.
Focant B., Joyeux J.C. (1988) Essai de spéciation biochimique de six espéces de Gobiidés du littoral Languedocien. Commission Internationale pour l'Exploration Scientifique de la Mer Méditerranée. Rapports et Procès-Verbaux des Réunions 31:257.
Focant B., Pequeux A. (1985) Comparative electrophoretic study of myosins and parvalbumins from three deep sea fishes: Mora moro R., Conocara murrayi K. and Coryphaenoides rupestris G. Bulletin de la Société Royale des Sciences de Liège 1:55-64.
Focant B., Vandewalle P. (1991) Comparison of myosin subunits and sarcoplasmic parvalbumins of white and red trunk muscles from various species of African Cichlids. Application to an hybrid. Musée Royal de l'Afrique Centrale, Tervueren, Belgique. Annales, Sciences Zoologiques 262:33-38.
Focant B., Huriaux F., Johnston I.A. (1976) Subunit composition offish myofibrils: the light chains of myosin. International Journal of Biochemistry 7:129-133.
Focant B., Jacob M.F., Huriaux F. (1981) Electrophoretic comparison of the proteins of some perch (Perca fluviatilis L.) head muscles. Journal of Muscle Research and Cell Motility 2:295-305.
Focant B., Viladiu C., Vandewalle P. (1988) Biochemical analysis of parvalbumins and myosin light chains from Mediterranean Serranids: first application to the systematic. Commission Internationale pour l'Exploration Scientifique de la Mer Méditerranée. Rapports et Procès Verbaux des Réunions 31:258.
Focant B., Michel C., Vandewalle P. (1990) Use of the biochemical analysis of muscle proteins to help the classification of polychromic individuals of the genus Symphodus. Archives Internationales de Physiologie et de Biochimie 98:87-93.
Focant B., Huriaux F., Vandewalle P., Castelli M., Goessens G. (1992) Myosin, parvalbumin and myofibril expression in barbel (Barbus barbus L.) lateral white muscle during development. Fish Physiology and Biochemistry.
Frankel J.S. (1983) Lactate dehydrogenase tissue specificity and characterization in the teleost genus Barbus. Comparative Biochemistry and Physiology 76 B:103-105.
Frankel J.S. (1985) Ontogenetic patterns of enzyme locus expression in Barbus hybrids (Cypriniformes, Teleostei). Comparative Biochemistry and Physiology 82 B:413-417.
Frankel J.S., Wilson R.V. (1984) Comparison of the spatial and temporal expression of supernatant malate dehydrogenase in Barbus hybrids (Cypriniformes, Teleostei). Comparative Biochemistry and Physiology 78 B:179-182.
Frankel J.S., Wilson R.V. (1985) Aberrant gene expression at the creatine kinase loci during Barbus hybrid development (Cypriniformes, Teleostei). Comparative Biochemistry and Physiology 80 B:463-466.
Gerday C. (1982) Soluble calcium‐binding proteins from fish and invertebrate muscle. Molecular Physiology 2:63-87.
Huriaux F., Focant B. (1977) Isolation and characterization of the three light chains from carp white muscle myosin. Archives Internationales de Physiologie et de Biochimie 85:917-929.
Huriaux F., Focant B. (1978) Effect of some factors on the molecular weight determination of a light chain (LC3) of carp (Cyprinus carpio L.) skeletal muscle myosin by SDS‐polyacrylamide gel electrophoresis. Comparative Biochemistry and Physiology 61 B:195-198.
Huriaux F., Focant B. (1985) Electrophoretic and immunological study of myosin light chains from freshwater teleost fishes. Comparative Biochemistry and Physiology 82 B:737-743.
Huriaux F., Lefèbvre F., Focant B. (1983) Myosin polymorphism in muscles of the toadfish, Opsanus tau. Journal of Muscle Research and Cell Motility 4:223-232.
Huriaux F., Vandewalle P., Philippart J.C., Focant B. (1990) Electrophoretic comparison of myosin light chains and parvalbumins of trunk and head muscles from two barbel (Barbus barbus) populations. Comparative Biochemistry and Physiology 97 B:547-553.
Huriaux F., Focant B., Vandewalle P. (1991) Spatial and temporal distribution of the parvalbumin isotypes in barbel muscles. Journal of Muscle Research and Cell Motility 12:114-115.
Huriaux F., Vandewalle P., Focant B. (1991) Myosin heavy chain isoforms in white, red and ventricle muscles of barbel (Barbus barbus L.). Comparative Biochemistry and Physiology 100 B:309-312.
Karasinski J., Kilarski W. (1989) Polymorphism of myosin isoenzymes and myosin heavy chains in histochemically typed skeletal muscles of the roach (Rutilus rutilus L., Cyprinidae, fish). Comparative Biochemistry and Physiology 92 B:727-731.
Laemmli U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
Martinez I., Ofstad R., Olsen R.L. (1990) Electrophoretic study of myosin isoforms in white muscles of some teleost fishes. Comparative Biochemistry and Physiology 96 B:221-227.
Martinez I., Ofstad R., Olsen R.L. (1990) Myosin isoforms in red and white muscles of some marine teleost fishes. Journal of Muscle Research and Cell Motility 11:489-495.
Ochiai Y., Watabe S., Hashimoto K. (1988) Physicochemical and immunological properties of myosin light chains from the ordinary muscle of marine teleost fishes. Comparative Biochemistry and Physiology 90 B:347-353.
Ochiai Y., Kobayashi T., Watabe S., Hashimoto K. (1990) Mapping of fish myosin light chains by two‐dimensional gel electrophoresis. Comparative Biochemistry and Physiology 95 B:341-345.
Perrie W.T., Perry S.V. (1970) An electrophoretic study of the low‐molecular‐weight components of myosin. Biochemical Journal 119:31-38.
Rowlerson A., Scapolo P.A., Mascarello F., Carpene E., Veggetti A. (1985) Comparative study of myosins present in the lateral muscle of some fish: species variations in myosin isoforms and their distribution in red, pink and white muscle. Journal of Muscle Research and Cell Motility 6:601-640.
Varma A.K., Frankel J.S. (1980) A comparison of tissue esterases in the genus Barbus by vertical gel electrophoresis. Comparative Biochemistry and Physiology 65 B:267-273.
Watabe S., Ochiai Y., Hashimoto K. (1982) Identification of 5,5′‐dithio‐bis‐2‐nitrobenzoic acid (DTNB) and alkali light chains of piscine myosin. NIPPON SUISAN GAKKAISHI 48:827-832.
Similar publications
Sorry the service is unavailable at the moment. Please try again later.
This website uses cookies to improve user experience. Read more
Save & Close
Accept all
Decline all
Show detailsHide details
Cookie declaration
About cookies
Strictly necessary
Performance
Strictly necessary cookies allow core website functionality such as user login and account management. The website cannot be used properly without strictly necessary cookies.
This cookie is used by Cookie-Script.com service to remember visitor cookie consent preferences. It is necessary for Cookie-Script.com cookie banner to work properly.
Performance cookies are used to see how visitors use the website, eg. analytics cookies. Those cookies cannot be used to directly identify a certain visitor.
Used to store the attribution information, the referrer initially used to visit the website
Cookies are small text files that are placed on your computer by websites that you visit. Websites use cookies to help users navigate efficiently and perform certain functions. Cookies that are required for the website to operate properly are allowed to be set without your permission. All other cookies need to be approved before they can be set in the browser.
You can change your consent to cookie usage at any time on our Privacy Policy page.