Comparative studies on immunochemical properties of female-specific serum protein and egg yolk proteins in rainbow trout (Salmo gairdneri)

Hara, Akihiko; Hirai, Hidematsu

doi:10.1016/0305-0491(78)90011-1

Cited by 64 publications

(32 citation statements)

References 20 publications

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“…When comparing the present results to those obtained by others, it appears that the distribution of the main components was similar, whatever the source of VTG : mature female trout (Hara and Hirai, 1978 ; this study) estrogenized male trout (Campbell and Idler, 1980), estrogenized juvenile trout (Norberg and Haux, 1985) or vitellogenic trout receiving an n-3 deficient or non-deficient diet (Fremont et al, 1984). Moreover, analyses performed during the last 5 months before ovulation did not show any change in the proportions of protein and lipid classes (Riazi and Fremont, 1988).…”

supporting

confidence: 83%

“…As reported by Hara and Hirai (1978), carbohydrates were present but they were minor components, comprising 0.3 % of VTG ; this content was lower than that of Xenopus VTG (Tata, 1976 (1980), Hara and Hirai (1978) for trout. The major amino acids were alanine, glutamic acid and leucine.…”

mentioning

confidence: 45%

“…Introduction. Vitellogenin (VTG), the lipophosphoprotein synthesized during vitellogenesis by oviparous vertebrates, has been characterized in some fish species including rainbow trout (Hara and Hirai, 1978;Campbell and Idler, 1980; Norberg and Haux, 1985). The complex is generally isolated by precipitation.…”

mentioning

confidence: 99%

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Biochemical analysis of vitellogenin from rainbow trout (Salmo gairdneri) : fatty acid composition of phospholipids

Frémont¹,

Riazi²

1988

Reprod. Nutr. Dévelop.

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Summary. Vitellogenin was obtained from three year-old vitellogenic trout.Two procedures of isolation were compared : dialysis against distilled water and ultracentrifugation in the density interval 1 .21 -1 .28 g/ml.Similar patterns were observed by gel filtration and electrophoresis for both preparations of vitellogenin, indicating that electric charge and molecular weight were not modified by either procedure.The apparent M, of the native form was 560,000 in gel filtration, whereas that of the monomer was estimated as 170,000 by sodium dodecylsulfate-polyacrylamide gel electrophoresis. Minor proteins were also detected (100,000-88,000-78,000).The main components were protein (79%), and lipids (19 %), Carbohydrates accounted for 0.3 % when protein phosphorus and calcium each represented 0.7 % of total weight.Phospholipids (70 % of total lipids) mainly consisted of phosphatidylcholine in which n-3 docosahexanenoic acid accounted for one-third of total fatty acids.The results show the high levels of essential fatty acids in structural lipids which are known to be involved in embryo development.Introduction.

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confidence: 83%

mentioning

confidence: 45%

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Biochemical analysis of vitellogenin from rainbow trout (Salmo gairdneri) : fatty acid composition of phospholipids

Frémont¹,

Riazi²

1988

Reprod. Nutr. Dévelop.

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“…It is well known that several female-specific serum proteins are immunochemically found at the vitellogenic stage in the teleost. [13][14][15][16] In the present study, the presence of three female-specific proteins was demonstrated and it was supposed that yolk protein might be composed of the major component since the ovarian extract was obtained from ovaries full of matured oocytes.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of a Yolk Protein from the Scallop Ovary.

Osada

Unuma

Mori

1992

NIPPON SUISAN GAKKAISHI

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A female specific protein (FSP) was identified and purified from the ovary of the Japanese scallop Patinopecten yessoensis by immunological techniques and a combination of precipitation with distilled water, ammonium sulfate fractionation, hydroxylapatite chromatography, and gel filtration. The molecular mass was determined to be approximately 450kDa. Three other female specific proteins, two with the same molecular mass and the other with 700kDa, showed different electrophoretic mobility from each other on native polyacrylamide gel electrophoresis, and reacted to antiserum against purified FSP (anti-FSP) by immunoblotting. No FSP was immunologically detected in the extract of the digestive diverticula or in the concentrated hemolymph. However, the extracts from the ovary of Chlamys farreri nipponensis and Mytilus edulis, though not those of Crassostrea gigas, reacted to anti-FSP. The amount of FSP in the ovarian extract from the scallop increased with the progressive growth of the oocytes and this protein wsa localized in the cytoplasm of the oocyte. It is assumed that the purified FSP is formed as a yolk protein in the ovary and the yolk protein is possibly composed of four molecules synthesized from the same source as this purified FSP, the antigenicity of which is partially maintained among bivalve species.

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“…This makes a necessary more in-depth study of Vtg for every species of fish. Even though Vtgs has been widely studied in different bony fish species (Hara & Hirai, 1978;De Vlaming et al, 1980;Mañanós et al, 1994;Palumbo et al, 2007;Zhong et al, 2014), in South American freshwater fish species it has been only carried out in Arapaima gigas and Rhamdia quelen (Chu-Koo et al, 2008;Mour-Costa et al, 2016). Proteomics tools such as two-dimensional gel electrophoresis and mass spectrometry have been shown to be very helpful to identify and characterize different Vtgs from plasma samples in fish (Cohen et al, 2005(Cohen et al, , 2009Palumbo et al, 2007), avoiding long and tedious purification processes.…”

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confidence: 99%

Proteomic characterization of vitellogenins from three species of South American fresh water fish

Urdaneta

Camafeita

Poleo

et al. 2018

lajar

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ABSTRACT. Vitellogenins (Vtg) are glycolipophosphoproteins synthesized by oviparous vertebrates as yolk proteins precursors. These proteins have been studied for their role in reproduction and in endocrine disruption. In this work, we report the first proteomic study towards the characterization of Vtg from Pseudoplatystoma fasciatum, Piaractus brachypomus and Colossoma macropomum. Male specimens of each of the three fish species were estradiol-induced (experimental) and non-induced (control). The initial Vtg characterization was made by 2D protein gel electrophoresis of both groups The identification of the high molecular weight spots, presumed to be Vtgs, was assessed by MALDI-TOF mass spectrometry analysis. A post-translational modification study was performed by differential staining of 2D gels in order to visualize phosphoproteins and glycoproteins. Plasma samples from the three species, induced with estrogen, showed three high molecular weight spots with variable isoelectric points. Post-translational modifications showed that Vtgs from P. brachypomus and C. macropomum presented a phosphorylated and glycosylated subunit, while the same subunit in P. fasciatum was only glycosylated. This characterization will help in the development of reliable immunoassays, which could be used for studies of endocrine disruption or for the improvement of artificial spawning, by uncovering the time of fish maturation or sex determination.

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Comparative studies on immunochemical properties of female-specific serum protein and egg yolk proteins in rainbow trout (Salmo gairdneri)

Cited by 64 publications

References 20 publications

Biochemical analysis of vitellogenin from rainbow trout (Salmo gairdneri) : fatty acid composition of phospholipids

Biochemical analysis of vitellogenin from rainbow trout (Salmo gairdneri) : fatty acid composition of phospholipids

Purification and Characterization of a Yolk Protein from the Scallop Ovary.

Proteomic characterization of vitellogenins from three species of South American fresh water fish

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