[Characteristics of heterogeneity of serum albumin in heterosis-hybrid chickens].
A comparative study was performed for isoelectric and electrophoretic spectra blood serum albumin of parental breeds of chickens and their heterosis hybrids --broiler cocks. The method of isoelectric focusing within the surcrose density gradient and pH 4-6 created by the gradient of sucrose, mannitol and boron-borate buffer (pH 8.5) concentrations was applied. The electrophoretic spectrum of the serum albumin fraction homogeneous in the agar gel was obtained by electrophoresis in 7% polyacrylamide gel. The isoelectric spectrum of heterosis hybrid albumin is established to be more heterogeneous and during isoelectric focusing it is divided within a range of pH 4.6-5.2 into seven fractions against four-five components of the parent breed albumin. Among them it is possible to distinguish the fraction involving more than 50% of the total protein (the great component) and some small components with different protein content and belonging wither to a more acid or more basic region as compared to pI of the great component. The pI value of the great component for hybrid albumin is shifted towards the acid region (4.76 against 4.85 and 5.07 in albumin of the parent breeds). Small component of hybrid albumin are characterized by an increase in their amount, but pI of the fraction is within the range of values peculiar to albumin of the maternal and paternal lines. The albumin preparations of all the studied chicken breeds isolated from blood serum by electrophoresis in the agar gel manifest multiplicity of the protein bands in a 7% polyacrylamide gel. The electric spectra of hybrid albumin and parent breeds albumin differ in the distribution pattern of the components and their quantitative composition. A relative electrophoretic mobility of the intensively stained dense band which represents the main electrophoretic component is increased in hydrid albumin with the respect to albumin of the maternal line but is identical to the paternal line.
[Characteristics of heterogeneity of serum albumin in heterosis-hybrid chickens]. A comparative study was performed for isoelectric and electrophoretic spectra blood serum albumin of parental breeds of chickens and their heterosis hybrids --broiler cocks. The method of isoelectric focusing within the surcrose density gradient and pH 4-6 created by the gradient of sucrose, mannitol and boron-borate buffer (pH 8.5) concentrations was applied. The electrophoretic spectrum of the serum albumin fraction homogeneous in the agar gel was obtained by electrophoresis in 7% polyacrylamide gel. The isoelectric spectrum of heterosis hybrid albumin is established to be more heterogeneous and during isoelectric focusing it is divided within a range of pH 4.6-5.2 into seven fractions against four-five components of the parent breed albumin. Among them it is possible to distinguish the fraction involving more than 50% of the total protein (the great component) and some small components with different protein content and belonging wither to a more acid or more basic region as compared to pI of the great component. The pI value of the great component for hybrid albumin is shifted towards the acid region (4.76 against 4.85 and 5.07 in albumin of the parent breeds). Small component of hybrid albumin are characterized by an increase in their amount, but pI of the fraction is within the range of values peculiar to albumin of the maternal and paternal lines. The albumin preparations of all the studied chicken breeds isolated from blood serum by electrophoresis in the agar gel manifest multiplicity of the protein bands in a 7% polyacrylamide gel. The electric spectra of hybrid albumin and parent breeds albumin differ in the distribution pattern of the components and their quantitative composition. A relative electrophoretic mobility of the intensively stained dense band which represents the main electrophoretic component is increased in hydrid albumin with the respect to albumin of the maternal line but is identical to the paternal line.