The electrophoretic mobility test with myelin basic protein, binding of125I-MBP to lymphocytes, and gel electrophoresis pattern of supernatant during incubation

1980 ◽  
Vol 177 (3) ◽  
pp. 245-253
Author(s):  
K. Mross ◽  
B. Mross ◽  
D. I. Wolfrum ◽  
A. Kohlschütter
1991 ◽  
Vol 39 (1) ◽  
pp. 111-121 ◽  
Author(s):  
W D Geoghegan

An electrophoretic method was developed to determine the conditions required for production of electrophoretically uniform protein-colloidal gold complexes from monodisperse colloidal gold (Au) and electrophoretically uniform protein. The method is based on the electrophoretic migration of protein-Au complexes in agarose. The results demonstrate that two variables, the pH of adsorption and the quantity of protein added, can be manipulated to vary the electrophoretic mobility of the resulting protein-Au complexes. Thus, agarose gel electrophoresis can be used to select the pH of adsorption and the quantity of protein required to produce electrophoretically uniform protein-Au complexes. This new electrophoretic mobility test can be used in place of or in addition to the classical procedure of Zsigmondy and its many variations, both visual and spectrophotometric. The procedure described is also useful for electrophoretic comparison of small quantities of various protein-Au samples.


The Lancet ◽  
1979 ◽  
Vol 313 (8126) ◽  
pp. 1138-1139 ◽  
Author(s):  
GeoffreyV.F. Seaman ◽  
RoyL. Swank ◽  
CherryH. Tamblyn ◽  
CharlesF. Zukoski

1982 ◽  
Vol 28 (4) ◽  
pp. 813-818 ◽  
Author(s):  
D E Comings ◽  
A Pekkula-Flagan

Abstract To examine the basic human brain proteins, we subjected 9 mmol/L urea extracts to non-equilibrium gel electrophoresis. The pattern observed differs distinctly from that with equilibrium gel electrophoresis. With this technique, the myelin proteins (myelin basic protein, proteolipids, and basic Wolfgram proteins) and many other unindentified major basic proteins can be demonstrated. The myelin basic proteins occur as two major polypeptides of different charge and slightly different molecular mass, indicating the action of at least two genes. The proteolipid proteins occur as a long series of charge isomers, suggesting multiple genes or extensive post-transcriptional modification. In one patient with schizophrenia, a charge-change mutation of the larger myelin basic protein (MBL) was observed and is termed "MBL-Duarte."


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