22 research outputs found

    Відділення фізики і астрономії Національної академії наук України

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    Developmental changes in myofibrillar protein composition were investigated in the myotomal muscle of the African catfish, Heterobranchus longifilis (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, α-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 H. longifilis 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

    Electrophoretic differentiation of the fibre types of adductor mandibulae, sternohyoideus and protractor hyoideus muscles of the carp (Cyprinus carpio L.)

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    peer reviewed1. 1. The estimation of relative proportions of white and red myosin light chains separated on PAGE allows the calculation of red fibre content of several carp head muscles. 2. 2. The muscle composition appears related to the function: muscle acting during slow respiratory movements possesses a higher amount of red fibres (A1β and A3). Moreover, most of the examined muscles are heterogeneous with a set of white fibres adjacent to red ones. 3. 3. Peculiar fibres observed in protractor hyoideus lateral: they show a white type myosin and contain a low amount of myoglobin while the parvalbumins and lactic dehydrogenase isoenzymes distributions are typical of the red type

    Immunological study of muscle parvalbumin isotypes in three African catfish during development

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    Eleven parvalbumin isotypes expressed during the development of clariids Heterobranchus longifilis and Clarias gariepinus and claroteid Chrysichthys auratus were purified and electrophoresed on sodium-dodecyl-sulfate polyacrylamide gels. Immunochemical cross-reactions among these proteins were investigated by immunoblotting, using purified antibodies raised against three isotypes chosen at different stages of fish development. Antibodies raised against H. longifilis PA I (larval-juvenile isotype) and against C. gariepinus PA IIIa (juvenile-adult isotype) cross-reacted to a rather similar extent despite a weaker cross-reaction of anti-PA IIIa with larval-juvenile isotypes. On the other hand, antibodies raised against H. longifilis PA IV (an exclusively adult isotype) recognized markedly only H. longifilis PA IV and C. gariepinus PA IIIb. These two adult isotypes most likely belong to the alpha lineage, and all the others to the P lineage. These results show that parvalbumin isotypes synthesized at different stages of fish growth differ structurally, and that the most marked difference is between larval-juvenile and adult clariid isotypes. (C) 2002 Elsevier Science Inc. All rights reserved

    Myosin heavy chain isoforms in white, red and ventricle muscles of barbel (Barbus barbus L.)

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    1. 1. Actomyosin extracts of trunk, heart, and head muscles from barbel (Barbus barbus L.) were analyzed by SDS-polyacrylamide gel electrophoresis to study their myosin heavy chain composition. 2. 2. Four heavy chain isoforms were found: trunk white, trunk red, and ventricle muscles yielded one heavy chain typical of the muscle type; head muscles devoid of red fibers displayed two heavy chain isoforms, the slow migrating one corresponding to the trunk white muscle type. 3. 3. The electrophoretic mobility of red and ventricle myosin heavy chains related to that of white isoforms appeared highly modified by the glycerol content of the gels

    Polymorphism of white muscle myosin and parvalbumins in the genus Barbus (Teleostei: Cyprinidae)

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    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

    Use of the biochemical analysis of muscle proteins to help the classification of polychromic individuals of the genus symphodus

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    Among Labrid fishes (Wrasses), polychromy is very frequent. Indeed, a few species of Symphodus show individuals with a peculiar colouration. On one hand, electrophoretic analysis of muscular proteins (myosin and parvalbumins) reveals no differences between the normal individuals and the coloured morphs of the three species. On the other hand, these analyses display disparities between fishes of the two subgenus (Crenilabrus and Symphodus). Biochemical characters seem to have evolved in the same way that morphological and behavioural ones: the subspecies based only on differences in colouration are not confirmed but the differences between subgenus are revealed

    Expression of myofibrillar proteins and parvalbumin isoforms during the development of a flatfish, the common sole Solea solea: Comparison with the turbot Scophthalmus maximus

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    peer reviewedDevelopmental changes in myofibrillar protein and parvalbumin isoform composition were investigated in the myotomal muscle of the flatfish Solea solea, characterized by a very brief metamorphic stage. Results were compared with previously obtained data on another pleuronectiform teleost, the turbot (Scophthalmus maximus), displaying prolonged metamorphosis. Electrophoretically measurable changes in myofibrillar proteins and parvalbumins were detected late in the sole, after completion of metamorphosis. In the course of development, muscles showed the usual sequential synthesis of isoforms of the myofibrillar proteins myosin light chain LC2, troponin-T, and troponin-I. An adult parvalbumin isoform (PA III) was found to predominate during sole growth. The two flatfish were characterized by highly species-specific parvalbumin isoforms. Compared with turbot, the profiles of the myofibrillar subunits and parvalbumin isoforms varied little in the course of sole development. The early appearance of adult traits might be correlated with the brevity of metamorphosis of this fish

    Biochemical attempt to characterize thirteen cichlid species by their muscular paralbumins

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    This paper shows the usefulness of polyacrylamide gel electrophoresis (PAGE) separation of a few well-characterized muscle proteins, the paralbumins, in the systematic study of 13 cichlid species. The separation of the isoforms of these abundant, quite species-specific fish paralbumins is fast, easy, and requires but small quantities of muscle material. Used alone, this technique suggests hypotheses for species classification. In conjunction with morphological analysis, it makes it possible to confirm or invalidate doubts about the determination

    Early development of the cephalic skeleton of Barbus barbus (Teleostei, Cyprinidae)

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    The inception, and development of the cephalic skeleton of Barbus barbus from hatching to 24 days passes through periods of fast and slow growth; these rates are not the same in different parts of the skull. Trabeculae, parachordal plates, Meckelian cartilages and hyposymplectics are present at hatching. Then the cartilaginous floor of the neurocranium develops, the pars quadrata, the hyoid bars and branchial arches elements appear shortly before the first movable dermal bones, the dentaries, maxillae and opercles. The first bone of the braincase to appear is the parasphenoid; other bones develop subsequently and at the same time: the angular, quadrate, interopercle and fifth ceratobranchial. Later the splanchnocranium continues to develop at a relatively fast rate while the neurocranium shows little growth. The braincase does not begin to close before the 24th day, nor do the first bones of the skull roof appear, while the bucco‐pharyngeal apparatus is complete, having the adult shape. The early constitution of the latter structures seems to be linked with the mechanical demands of biological functions such as breathing and feeding

    Postembryonic development of the cephalic skeleton in Dicentrarchus labrax (Pisces, Perciformes, Serranidae)

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    peer reviewedAt hatching, Dicentrarchus labrax larvae are 3.0 mm long and devoid of any cephalic skeleton. At 3.6 mm, the Meckelian cartilage appears, after which the whole skeleton develops so slowly and gradually that clear-cut stages are impossible to define. Some cephalic elements, however, develop faster than others. Skeletal development is subject to constraints imposed by vital functions such as aquatic respiration and feeding. As the yolk sac shrinks, the branchial parts develop. By the time the vitellus is completely exhausted, the mandible, pharyngeal jaws, hyoid bar, and parts of the suspensorium and operculum are present. Though still incomplete, these structures are probably sufficient to allow ingestion of exogenous food. Further development should enable the larvaes to perform suction feeding, as is typical of perciforms. Before the shift to exogenous feeding, the cartilaginous floor of the skull remains open, but the opening is then closed by the parasphenoid and basioccipital, so the brain is completely isolated from the buccal cavity. The cranial vault and ethmoid region develop later: these structures are probably less essential to fry survival than the earlier and more rapidly developing structures
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