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Veterinary clinical pathology, 2019
Protein electrophoresis and immunotyping can be a useful adjunct to the standard biochemical techniques for characterizing serum and urine proteins. This paper reviews currently available and commonly used methods for diagnostic protein electrophoresis ...
A. R. Moore, Paul R. Avery
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Protein electrophoresis and immunotyping can be a useful adjunct to the standard biochemical techniques for characterizing serum and urine proteins. This paper reviews currently available and commonly used methods for diagnostic protein electrophoresis ...
A. R. Moore, Paul R. Avery
semanticscholar +1 more source
The Nurse Practitioner, 1982
More than 100 serum proteins have been biochemically identified; relatively few have well-documented clinical significance. In an effort to discriminate between healthy and diseased individuals, investigators have studied many protein levels and patterns from birth throughout life.
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More than 100 serum proteins have been biochemically identified; relatively few have well-documented clinical significance. In an effort to discriminate between healthy and diseased individuals, investigators have studied many protein levels and patterns from birth throughout life.
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2003
Serum protein electrophoresis (SPE) is a technique that has been used in clinical laboratories for several decades to elucidate and quantitate monoclonal paraproteins. These proteins are indicative of patients with a B-cell dyscrasia, which, if untreated, could lead to the early demise of the patient.
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Serum protein electrophoresis (SPE) is a technique that has been used in clinical laboratories for several decades to elucidate and quantitate monoclonal paraproteins. These proteins are indicative of patients with a B-cell dyscrasia, which, if untreated, could lead to the early demise of the patient.
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Capillary electrophoresis of recombinant proteins
Journal of Chromatography B: Biomedical Sciences and Applications, 1997Many naturally occurring proteins which are used therapeutically have been cloned and expressed in large quantities in bacterial, yeast or mammalian systems. Purification of these proteins by column chromatography generates high purity products with low levels of host protein contaminants.
K A, Denton, S A, Tate
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Capillary Electrophoresis of Proteins
1995Because of the developments in biotechnology, e. g., the introduction of recombinant protein technology, there is an increasing demand for suitable separation techniques for biomolecules. Up-scaling is required for preparative purposes such as purification or for subsequent structural analysis, while down-scaling to miniaturized dimensions is needed to
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Electrophoresis of cereal storage proteins
Journal of Chromatography A, 2000Cereal proteins have been studied by a number of analytical techniques over the years. One of the major methodologies utilized by cereal chemists has been electrophoresis. Starting with moving boundary electrophoresis and progressing to slab gels and high-performance capillary electrophoresis, innovative methods have been developed to provide high ...
S R, Bean, G L, Lookhart
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Fruit proteins: Extraction and electrophoresis
Analytical Biochemistry, 1965Abstract A technique has been developed for preparation of powders of fruit tissues for protein studies. The procedure involves rapid freezing of tissue in acetone at −70°C, followed by comminution in the acetone at this temperature. Upon elevation of the temperature to −25°, water passes into the acetone, and the liquid phase is drawn off through an
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Serum protein electrophoresis in brucellosis
Transactions of the Royal Society of Tropical Medicine and Hygiene, 1959Abstract 1. 1) Quantitative fractionation of the serum proteins was carried out in brucellosis by the filter paper electrophoretic method. The changes in the serum protein fractions were followed in patients suffering from Brucella melitensis infection, either in its acute stages or during relapses.
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Semipreparative electrophoresis with prestained proteins
Analytical Biochemistry, 1979Abstract A simple method for prestaining proteins with Coomassie blue G prior to acrylamidegel electrophoresis is described. Many, although not all, undenatured proteins can be stained. This prestaining technique can be conveniently coupled with a second electrophoresis step, using Sephadex as a supporting medium, to yield isolated protein in about 4
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