Disc electrophoresis of plasma proteins of fish. physical and chemical characters; localization of fibrinogen, transferrin and ceruloplasmin in the plasma of the rainbow trout (Salmo gairdnerii Richardson)
“…Whereas some authors advocate using the human electrophoretic pattern (Schlotfeldt, 1975), others reject this practice (Post, 1966;Perrier et al, 1974), because neither the number nor the mobility of the protein fractions correspond in rainbow trout and human sera. Indeed, Post (1 966) demonstrated that in rainbow trout, humoral antibodies migrate in the slowest moving fraction.…”
Section: Electrophoretic Separation Of Serum Constituentsmentioning
confidence: 95%
“…Nevertheless, there is no full comparison with regard to the quantity and character of albumin proportions. The number of albumin fractions recorded on CA and PAA/PAGE carriers fluctuated from one to three (Hara, 1975;Borchard, 1978;Perrier et al, 1974). Kirsipuu (1979) subjected each fraction of the paper electropherogram to a second electrophoresis on PAA/PAGE gel.…”
Section: Electrophoretic Separation Of Serum Constituentsmentioning
The literature on the blood chemistry of rainbow trout, Sulrno guirdneri Rich., is reviewed from the aspects of experimental methods, electrophoresis, normal values, environmental and endogenous factors including toxic substances and diseases.
“…Whereas some authors advocate using the human electrophoretic pattern (Schlotfeldt, 1975), others reject this practice (Post, 1966;Perrier et al, 1974), because neither the number nor the mobility of the protein fractions correspond in rainbow trout and human sera. Indeed, Post (1 966) demonstrated that in rainbow trout, humoral antibodies migrate in the slowest moving fraction.…”
Section: Electrophoretic Separation Of Serum Constituentsmentioning
confidence: 95%
“…Nevertheless, there is no full comparison with regard to the quantity and character of albumin proportions. The number of albumin fractions recorded on CA and PAA/PAGE carriers fluctuated from one to three (Hara, 1975;Borchard, 1978;Perrier et al, 1974). Kirsipuu (1979) subjected each fraction of the paper electropherogram to a second electrophoresis on PAA/PAGE gel.…”
Section: Electrophoretic Separation Of Serum Constituentsmentioning
The literature on the blood chemistry of rainbow trout, Sulrno guirdneri Rich., is reviewed from the aspects of experimental methods, electrophoresis, normal values, environmental and endogenous factors including toxic substances and diseases.
“…The results are similar to those found in frogs (Badawy and Evans 1976) and rainbow trout fry weighing 13.60 to 49.43 g (Walton et al 1984), but are very different to those reported in mammals. In fish, particularly in rainbow trout, the lack of a link between Try and albumin could be related to the fact noted by Perrier et al (1974Perrier et al ( , 1977 that 0. mykiss albumin has physico-chemical properties different from those of human albumin. Moreover, in fish the percentage of albumin in serum is lower compared to the percentage of total serum protein (Sulya et al 1961).…”
The levels of tryptophan (Try), 5-hydroxytryptamine (serotonin, 5-HT) and 5-hydroxyindoleacetic acid (5-HIAA) were determined in the brain regions of rainbow trout (Oncorhynchus mykiss) by high performance liquid chromatography with electrochemical detection (HPLC-EC). Brain tryptophan concentrations varied from 3.972 ± 357 ng/g cerebellum) to 8.841 ± 772 ng/g (hypothalamus). The 5-HT concentrations varied from 69 ± 7 ng/g (optic tectum) to 573 ± 34 ng/g (hypothalamus). The concentrations of 5-HIAA varied from 29 ± 3 ng/g (medulla oblongata) to 68 ± 7 ng/g (hypothalamus). Total and free serum tryptophan levels were also determined; in adult rainbow trout 92% of the serum tryptophan was observed to be free i.e., not protein-bound.
“…In the case of fish plasma protein, the shortage of data makes the establishment of a pattern a quite difficult task, even within the same family (Perrier et al 1974). In addition, the concentration of these proteins can vary at any one time as it is affected by nutritional, physiological, and/or geographic conditions.…”
The interaction of methyl-parathion with the albumin of Piaractus mesopotamicus (Holmberg 1887) (= pacu), a fish species typical of Brazilian rivers, was studied and the results compared with known values for human and bovine albumin obtained in an earlier investigation. Methyl-parathion (O,O-dimethyl O-p-nitrophenyl phosphorothioate) is an organophosphorous pesticide still used in agriculture and fish farming in many countries. The fluorescence quenching technique with tryptophan as a natural probe was used to detect for the presence of methyl-parathion. Fluorescence can be mathematically expressed by the Stern-Volmer equation to calculate quenching constants, and changes in the behavior of Stern-Volmer curves at different temperatures indicate the nature of the mechanism causing the quenching. Our results indicate that methyl-parathion forms a complex with fish albumin. The estimated association constant is 9.73 x 103 (+/- 4.9 x 102) M(-1) at 25 degrees C.
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