Electrophoresis of Purified Antibody Preparations
ثبت نشده
چکیده
In connection with a study of the ultracentrifugal sedimentation of antibody preparations (1) the opportunity arose for study of the electrophoretic properties of some of the highly active material under investigation. Measurements of this kind are of value in the characterization of proteins and similar high molecular substances, and may also give information regarding the chemical homogeneity of the material, as shown in previous publications (2a). The measurements given in the present paper form part of a more detailed, as yet uncompleted investigation of the electrochemical properties of proteins in normal and immune sera. Since, however, the ultracentrifugal study referred to above was made on the same material, it was thought advisable to publish the electrophoretic data at the present time. Of the material used in the work of Heidelberger and Pedersen the following was investigated.
منابع مشابه
Electrophoresis of Purified Antibody Preparations
Electrophoretic mobilities of antibody preparations isolated from type specific antipneumococcus horse and rabbit sera, measured over a range of pH values, show that these preparations are distinctly different from normal serum proteins in their electrochemical properties.
متن کاملAN ELECTROPHORETIC STUDY OF IMMUNE SERA AND PURIFIED ANTIBODY PREPARATIONS*t
Studies on the eleetrophoresis of serum have shown that besides the albumin normal sera possess three separate globulin components differing in mobility and designated as cz, /3, and ~' (1). The relationship of antibodies to these components is of considerable importance. Differences in the antibody globulin formed in various animal species have already been found by ultracentrifugal studies (2...
متن کاملStructural relation between HDL-binding proteins in porcine liver.
We have found strong evidence for a relation between three high-density lipoprotein (HDL)-binding proteins of 90, 110, and 180 kDa in porcine liver that were detected by ligand blotting. Because HDL-binding proteins with identical molecular masses were detected in human liver, all subsequent experiments were performed with porcine liver proteins. An antiserum raised against a highly purified pr...
متن کاملRecognition of a 56 kDa protein in partially purified rat hepatic nuclear thyroid hormone receptor by anti-human c-erb A beta antibody.
Human beta thyroid hormone receptor (c-erb A beta protein) produced by an Escherichia coli expression system was purified by sequential column chromatography followed by electroelution from an electrophoresis gel and an antibody was prepared. The antibody recognized a 56 kDa protein band in a partially purified rat hepatic nuclear thyroid hormone receptor fraction on Western blotting. Although ...
متن کاملProduction and purification of polyclonal antibody against F(ab')2 fragment of human immunoglobulin G
Antibodies are essential tools of biomedical and biochemical researches. Polyclonal antibodies are produced against different epitopes of antigens. Purified F(ab')2 can be used for animal’s immunization to produce polyclonal antibodies. Human immunoglobulin G (IgG) was purified by ion exchange chromatography method. In all stages verification method of the purified antibodies was sod...
متن کاملA placental polypeptide activator of a membranous protein kinase and its relation to histone 1.
Crude transforming growth factor preparations of placenta contain a polypeptide that is required for the activity of a protein kinase that has been purified from plasma membrane preparations of Ehrlich ascites tumor cells. The kinase activator has been separated from transforming growth factor beta by reversed-phase HPLC and affinity chromatography. Like the transforming growth factor, it is he...
متن کامل