[Blood serum proteins detected by the method of disc electrophoresis in polyacrylamide gel].
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Color marker
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The protein spectrum of rat blood serum was studied by disc-electrophoresis in polyacrylamide gel. The obtained proteinograms of the blood serum contained 16-18 protein fractions which were identified for haptoglobin, ceruloplasmin, transferrin; the coefficient of mobility for albumin was also calculated for them. The rat blood serum proteinogram and the human blood serum proteinogram obtained under analogous conditions of electrophoresis are discussed for their peculiarities and similarity.
Haptoglobin
Ceruloplasmin
Blood serum
Serum Albumin
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Bovine serum albumin
Polyacrylamide
Protein purification
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Abstract Four different sample treatments (ethanol precipitation, dialysis, ultrafiltration, and gel filtration) to isolate cider proteins were tested in this work. Purified cider proteins were analyzed by capillary sieving electrophoresis (CSE) using linear polyacrylamide as a sieving medium under optimized conditions; with this technique, separation, and molecular weight determination of proteins are possible. The electropherograms obtained in the protein analysis with each treatment were compared to choose the one that led to the best results. This was found to be ultrafiltration; many peaks were obtained in the electrophoretic profile and their spectra corresponded to a protein. Bradford analysis confirmed this choice. These results were compared with those obtained by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE), the molecular weights of the protein bands agreeing with the molecular weights of the electrophoretic peaks obtained with ultrafiltration.
Ultrafiltration (renal)
Electropherogram
Sodium dodecyl sulfate
Ethanol precipitation
Molecular mass
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Haptoglobin
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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.
Polyacrylamide
Free-flow electrophoresis
Molecular-weight size marker
Difference gel electrophoresis
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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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Journal Article Electrophoresis of Serum Proteins in Acrylamide Gel: II. An Improved Apparatus and Technic for the Removal of Background Stain, by Means of an Electric Current Get access Thomas G. Ferris, LCDR, MSC, USNR, Thomas G. Ferris, LCDR, MSC, USNR 1Rear Admiral George W. Calver's Physical Chemistry Research Laboratory, Room 322, U. S. Naval Medical School, National Naval Medical Center, Bethesda 14, Maryland Search for other works by this author on: Oxford Academic Google Scholar Robert E. Easterling, HM1, USN, Robert E. Easterling, HM1, USN 1Rear Admiral George W. Calver's Physical Chemistry Research Laboratory, Room 322, U. S. Naval Medical School, National Naval Medical Center, Bethesda 14, Maryland Search for other works by this author on: Oxford Academic Google Scholar Richard E. Budd, HMC, USN Richard E. Budd, HMC, USN 1Rear Admiral George W. Calver's Physical Chemistry Research Laboratory, Room 322, U. S. Naval Medical School, National Naval Medical Center, Bethesda 14, Maryland Search for other works by this author on: Oxford Academic Google Scholar American Journal of Clinical Pathology, Volume 39, Issue 2_ts, February 1963, Pages 193–197, https://doi.org/10.1093/ajcp/39.2_ts.193 Published: 01 February 1963 Article history Received: 15 July 1962 Accepted: 15 October 1962 Published: 01 February 1963
George (robot)
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Blood protein electrophoresis
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