Polymorphism of myofibrillar proteins in histochemically identified myotomal muscle fibre types of <i>Heteropneustes fossilis</i> (Bloch) and <i>Labeo rohita</i> (Hamilton)

Jasra, Pardeep; Talesara, C. L.; Kiran, Shashi

doi:10.1111/j.1095-8649.1991.tb03103.x

Cited by 6 publications

(7 citation statements)

References 18 publications

(12 reference statements)

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“…Our findings are in line with the finding of Jasra et al [21] for myofibril proteins. They isolated myosin light chain, tropomyosin, Troponin-C and m-protein specifically from the muscle fibers of two freshwater fish species, viz., Heteropneustes fossils (Bloch) and L. rohita (Hamilon).…”

Section: Discussionsupporting

confidence: 96%

Phylogenetic Relationship of Cultured and WildLabeo rohitaandCirrhinus mrigalaBased on Muscles Proteins Profile in Different Weight Groups: A New Tool in Phylogenetic Analysis

Mahboob

Farooq

Mahmood

et al. 2012

International Journal of Food Properties

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Genetic heterogeneity and polymorphism in muscle proteins present in the meat of wild and cultured Labeo rohita and Cirrhinus mrigala was performed using SDS-PAGE. Cultured L. rohita and C. mrigala possessed more proteins than those in the wild ones and were dependent on their weight. Un-weighed pair group method with arithmetic average cluster analysis delineated a 50% linkage distance. Fish weight dissimilarity coefficient ranged from 1.73 to 3.87 in eight clusters at 75% linkage distance. The overall grouping pattern of clusters corresponded well with principal co-ordinate analysis and confirmed overall patterns of genetic variability among these species. These results provide useful guidelines for conservation and characterization of fish genetic resources for mass rearing or marker assisted breeding.

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Section: Discussionsupporting

confidence: 96%

Phylogenetic Relationship of Cultured and WildLabeo rohitaandCirrhinus mrigalaBased on Muscles Proteins Profile in Different Weight Groups: A New Tool in Phylogenetic Analysis

Mahboob

Farooq

Mahmood

et al. 2012

International Journal of Food Properties

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“…In R1 fibres, the most numerous, the m‐ATPase reacted negatively after alkaline pre‐incubation, and was stable after acid pre‐incubation. This behaviour is similar to that found in other teleosts ( Higgins 1990; Jasra et al . 1991 ).…”

Section: Discussionsupporting

confidence: 92%

Lateral Musculature in the Whitemouth Croaker (Micropogonias furnieri): its Characterization with Respect to Different Gonadal Conditions

Devincenti

Díaz

Goldemberg

2000

Anat Histol Embryol

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Histochemical and ultrastructural studies were performed on the lateral musculature from individual female whitemouth croaker, Micropogonias furnieri, at the anterior, medium and posterior regions. Based upon histochemical myosin-ATPase (m-ATPase) determination, diverse types of red, pink and white fibres were discerned. Red muscle had abundant mitochondria and stained intensely for aerobic enzymes, white muscle scarcely stained for the same enzymes and pink muscle responded in an intermediate manner. Both white and pink muscle had few mitochondria. The relative proportion of red muscle increased towards the caudal region; pink muscle diminished towards this region and white muscle modified its proportion only in the anterior region. m-ATPase activity showed differences in relation to the gonadal condition along the body, particularly in the white fibres at the anterior and medium regions.

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“…The activity of the mitochondrial enzyme SDH decreased rapidly in all samples. Such oxidative enzymes deteriorate fast during post mortem storage 2, 8, 25, 37. The enzyme Ca 2+ m‐ATPase also showed decreased activity in the various samples.…”

Section: Discussionmentioning

confidence: 98%

“…A 50 µg protein sample was loaded in each of the lanes. Electrophoresis was basically performed according to the procedure of Laemmli24 using 80 g L −1 separating gels and 30 g L −1 stacking gels 25. Protein standards were run simultaneously to determine the relative migrations of myofibrillar proteins.…”

Section: Methodsmentioning

confidence: 99%

Cryoprotective additives and cryostabilisation effects on muscle fillets of the freshwater teleost fish Rohu carp (Labeo rohita) during prolonged frozen storage

Jasra¹,

Zielinski²,

Jasra³

2006

J Sci Food Agric

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The effects of various cryoprotective additives separately and in combination were studied on the myofibrillar protein integrity, biochemical enzyme activity levels and muscle ultrastructure in the freshwater teleost fish Rohu carp (Labeo rohita). Fish muscle samples were divided into eight groups and immersed in different mixtures of cryoprotective additives (S1-S8), then frozen at −20 or −30 • C for 24 months. Electrophoretic studies revealed early (within 6 months) alteration of the myofibrillar proteins myosin light chain, α-actinin and tropomyosin. Reduction of the storage temperature from −20 to −30 • C slowed down the degradative processes. Sodium dodecyl sulfate polyacrylamide gel electrophoresis indicated that fish muscle treated with cryoprotective mixture S8 (40 g L −1 sorbitol/3 g L −1 sodium tripolyphosphate/4 g L −1 sodium alginate) showed minimal post mortem changes in myofibrillar proteins. Ultrastructural results also revealed post mortem damage to the muscle, seen earliest (within 6 months) in the sample frozen-stored without additives (S2), as compared with the normal, unfrozen muscle (S1). The influence of cryoprotectants alone and in combination on fish muscle structural proteins, myosin and actin filaments (A and I bands), during prolonged frozen storage was investigated. After 12 months, samples frozen-stored with various cryoprotective additives (S2-S7), except S8, showed signs of myofibrillar disintegration. Beyond that time the degradative processes started showing up in all samples, with minimal muscle ultrastructural damage in sample S8. Again, reducing the storage temperature from −20 to −30 • C slowed down the degradative processes. Ultrastructural results correlated well with levels of biochemical enzymes (Ca 2+ myofibrillar ATPase and succinic dehydrogenase) during frozen storage. This is the first report of the cryoprotective effects of these additives on this popular edible fish species. Of the various combinations of additives tested, cryoprotective mixture S8 was found to preserve the muscle structure longest under frozen storage conditions. However, even this mixture was only effective for 18 months at −30 • C. Beyond that time the myofibrillar degradative processes were apparent with correlative electrophoretic, biochemical and ultrastructural studies.

show abstract

Polymorphism of myofibrillar proteins in histochemically identified myotomal muscle fibre types of Heteropneustes fossilis (Bloch) and Labeo rohita (Hamilton)

Cited by 6 publications

References 18 publications

Phylogenetic Relationship of Cultured and WildLabeo rohitaandCirrhinus mrigalaBased on Muscles Proteins Profile in Different Weight Groups: A New Tool in Phylogenetic Analysis

Phylogenetic Relationship of Cultured and WildLabeo rohitaandCirrhinus mrigalaBased on Muscles Proteins Profile in Different Weight Groups: A New Tool in Phylogenetic Analysis

Lateral Musculature in the Whitemouth Croaker (Micropogonias furnieri): its Characterization with Respect to Different Gonadal Conditions

Cryoprotective additives and cryostabilisation effects on muscle fillets of the freshwater teleost fish Rohu carp (Labeo rohita) during prolonged frozen storage

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