“…In addition, our results with rainbow trout suggest that the two proteins previously referred to as para-albumins [6] are fatty-acid binding proteins and should thus simply be called albumins.…”
Section: Discussionmentioning
confidence: 87%
“…Albumin-like proteins were reported in lampreys on the basis of electrophoresis but these proteins did not bind fatty acids [12]. Studies on the serum proteins of rainbow trout have given conflicting views [5,6] but it has been proposed that the term para-albumin be given to the second and third most anodally migrating proteins based on their low molecular masses, lack of carbohydrate staining, solubility in ammonium sulphate, and electrophoretic mobilities [6]. We have used a physiological property of albumin, namely the ability to bind fatty acids [7,8], to identify plasma proteins in salmonids that appear to satisfy the standard criteria of serum albumin.…”
Section: Discussionmentioning
confidence: 99%
“…Other studies on carp plasma indicated that there were five proteins ranging in molecular mass from 145 to 58 kDa that had some properties in common with human albumin [4]. Initial characterisation of the plasma proteins of rainbow trout appeared to confirm the absence of an albumin-like fraction [5] but this was subsequently revised and two proteins were described as 'para-albumins' based on their molecular masses, electrophoretic mobilities, solubility in ammonium sulphate, and lack of glycoprotein staining [6]. One of the major physiological functions of albumin is to transport free fatty acids [7,8].…”
There has been considerable controversy over the existence of serum albumin in fish. One of the physiological functions of albumin is to bind free fatty acids. This characteristic was used to screen the plasma of seven species of salmonids. Each species contains a protein fraction that (i) binds palmitate, (ii) has a molecular mass similar to that of human serum albumin, and (iii) is one of the most rapidly migrating proteins when salmonid plasma is subjected to anodal polyacrylamide gel electrophoresis.We conclude therefore, that salmonids have serum albumins that are homologous to the serum albumin of higher vertebrates.
“…In addition, our results with rainbow trout suggest that the two proteins previously referred to as para-albumins [6] are fatty-acid binding proteins and should thus simply be called albumins.…”
Section: Discussionmentioning
confidence: 87%
“…Albumin-like proteins were reported in lampreys on the basis of electrophoresis but these proteins did not bind fatty acids [12]. Studies on the serum proteins of rainbow trout have given conflicting views [5,6] but it has been proposed that the term para-albumin be given to the second and third most anodally migrating proteins based on their low molecular masses, lack of carbohydrate staining, solubility in ammonium sulphate, and electrophoretic mobilities [6]. We have used a physiological property of albumin, namely the ability to bind fatty acids [7,8], to identify plasma proteins in salmonids that appear to satisfy the standard criteria of serum albumin.…”
Section: Discussionmentioning
confidence: 99%
“…Other studies on carp plasma indicated that there were five proteins ranging in molecular mass from 145 to 58 kDa that had some properties in common with human albumin [4]. Initial characterisation of the plasma proteins of rainbow trout appeared to confirm the absence of an albumin-like fraction [5] but this was subsequently revised and two proteins were described as 'para-albumins' based on their molecular masses, electrophoretic mobilities, solubility in ammonium sulphate, and lack of glycoprotein staining [6]. One of the major physiological functions of albumin is to transport free fatty acids [7,8].…”
There has been considerable controversy over the existence of serum albumin in fish. One of the physiological functions of albumin is to bind free fatty acids. This characteristic was used to screen the plasma of seven species of salmonids. Each species contains a protein fraction that (i) binds palmitate, (ii) has a molecular mass similar to that of human serum albumin, and (iii) is one of the most rapidly migrating proteins when salmonid plasma is subjected to anodal polyacrylamide gel electrophoresis.We conclude therefore, that salmonids have serum albumins that are homologous to the serum albumin of higher vertebrates.
“…In contrast, quantitative analysis with physicochemical reactions resulted in albumin portions of up to 32 per cent of total plasma protein (Ahne et al, 1976). Perrier et al (1974Perrier et al ( , 1977 suggested the term 'para-albumin' for the fast-moving fractions of rainbow trout electropherogram, because their physico-chemical properties differed from these of human albumin. Perrier et al (1 974, 1976aPerrier et al (1 974, , 1978c electrophoretically localized fibrinogen, ceruloplasmin and iodurophorine.…”
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.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.