[The differentiation of animal proteins using vertical polyacrylamid gel electrophoresis. 4. Serum proteins of the Carnivora].
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Serum protein pattern was studied in the leprosy spectrum, their contacts and in normal individuals by employing polyacrylamide gel electrophoresis. Sera from 80% of untreated BL/LL, 70% of untreated TT/BT patients and 67% of contacts have shown dysproteinaemia either for 232 kD or for 175 kD or for both these proteins together. Tendency of these proteins to return to normal levels was observed after treatment. But both these proteins come back to normal levels only after subsidence of the disease.
Polyacrylamide
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A technique of two-dimensional polyacrylamide gel electrophoresis for the separation of plasma proteins was described in detail. Human plasma proteins were separated by isoelectric focusing followed by electrophoresis in a 4 to 21% or a 4 to 30% linear gradient slab gel. Urea or SDS was not used throughout the procedure, so that the analyses of proteins in their biologically active state were possible. By this technique, human plasma protein was resolved into more than 250 spots.
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Objective To optimize the conditions for serum protein two-dimensional gel electrophoresis(2-DE)in peripherally venous blood of human being.Methods After albumin,IgG and salt were removed from serum samples,immobilized pH gradient isoelectric focusing(IEF)and vertical sodium dodecyl sulfonate polyacrylamide gel electrophoresis(SDS-PAGE)were applied to separate proteins.The amount of protein sample,pH range of IPG,the concentration of gel,the volume of sample hydration fluid,the IEF process parameters and other conditions were improved.Results With the conditions of dissolving 50 μg to100 μg proteins to form 350 μl sample fluid hydration,adjusting IPG pH from 4 to 7 and using 12% SDS-PAGE gel,as well as optimizing electrophoresis current,time and other parameters,suitable conditions for 2-DE were established and some ideal two dimensional maps of proteins were acquired.Conclusion The optimizated conditions for serum protein 2-DE in human being are the foundation for further study on serum differential proteomics.
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Abstract Purification of proteins from human plasma is a herculean task to perform 2-D gel electrophoresis. Human plasma contains nearly 70% albumin and globulin. The removal of such high abundance high molecular weight proteins is very difficult before performing 2-D gel electrophoresis. It becomes more difficult when we intent to investigate in infectious diseases like HIV/AIDS. We tried to the best of our efforts adopting various organic and non-organic based protocols based on various published papers. After failure of these protocols in results of 2-D gel-electrophoresis Aurum serum mini kit (Bio-Rad, USA) was adopted for plasma protein purification for performing 2-D gel electrophoresis. The low-abundance proteins were better resolved by 10% SDS-PAGE in 2-D gel-electrophoresis. Then,we extended the MALDI-TOF/TOF analysis of low-abundance proteins in human plasma by adopting the Aurum serum mini kit (Bio-Rad, USA) for 2-D gel electrophoresis. Thus, we concluded that, depletion of high abundant proteins like albumin and globulin, the use of the Aurum serum mini kit (Bio-Rad, USA) is the protocol of choice to perform the 2-D gel electrophoresis of HIV-1 infected human plasma.
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Protein spectra of blood serum were studied in 25 children suffering from phenlyketonuria (PKU) by disc electrophoresis in polyacrylamide gel. 14 children were examined in the course of being given a specialized diet on the basis of berlafen and 11 children were examined after they were switched over to common diet. PKU patients had an increased protein content in the zone of transferrins. After switching over to common diet the patients demonstrated the reduced protein content, increased amount of postalbumins of medium and low electrophoretic mobility, and transferrins as well.
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Color marker
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The electrophoertograms of protein of serum in Shan pig were analysed by the method of polyacrylamide gel electrophoresis. The result showed that the serum proteins, such as Pa, albemoglobin ( Alb ) , Po were separated into 4 ～ 6 zones, and Tf into 2～3 zones. The average molecular weight of albemoglobin (Alb) was about 69000 Da and Tf about 88000 Da. The separating of serum protein by polyacrylamide gel electrophoresis had fairly good repeated results and resolution ratio. The polymorphism and molecular weight of percentage in protein had important meanings for the hereditary feature analysis,breed choose and diseases diagnasis of the pigs.
Polyacrylamide
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The red blood cell membrane proteins of normal and spontaneous hypertensive Rats were studied by gradient polyacrylamide gel electrophoresis. The electrophoretic patterns of membrane proteins of hypertensive rats show three new bands of 58,000, 24,000 and 22,000 dalton. The existence of these new bands is not correlated with the age and the blood pressure values of the animals.
Cell membrane
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