Evidence for Specific Polypeptide Chain Folding in Myelin Basic Protein from Reactions Between Fragments of the Protein and Monoclonal Antibodies

2006 ◽  
Vol 47 (3) ◽  
pp. 764-771 ◽  
Author(s):  
Ellsworth C. Alvord ◽  
Sarka Hruby ◽  
Russell E. Martenson ◽  
Gladys E. Deibler ◽  
Mona J. Law
1988 ◽  
Vol 19 (4) ◽  
pp. 305-315 ◽  
Author(s):  
Nigel Groome ◽  
Adrian Dawkes ◽  
Richard Barry ◽  
Sarka Hruby ◽  
Ellsworth Alvord

1987 ◽  
Vol 24 (12) ◽  
pp. 1359-1364 ◽  
Author(s):  
S HRUBY ◽  
E ALVORDJR ◽  
N GROOME ◽  
A DAWKES ◽  
R MARTENSON

1978 ◽  
Vol 31 (11) ◽  
pp. 2367 ◽  
Author(s):  
BE Chapman ◽  
WJ Moore

Carbon-13 n.m.r, spectra have been obtained for bovine myelin basic protein at pD 4.4 in D2O and in 6 M guanidine deuterochloride solutions. Chemical-shift differences between resonances from some amino acid residues are interpreted in terms of structured regions in the polypeptide chain of the native protein, whereas the denatured protein displays the spectrum expected for an essentially random coil. Measurements of T1 and n.O.e. provide quantitative data on the dynamics of the backbone and side-chain carbons, and give support to the conclusion that the native protein does not have a random-coil structure.


2000 ◽  
Vol 122 (3) ◽  
pp. 429-436 ◽  
Author(s):  
R. Chignola ◽  
T. Cestari ◽  
C. Guerriero ◽  
A. P. Riviera ◽  
S. Ferrari ◽  
...  

1982 ◽  
Vol 41 (3) ◽  
pp. 355 ◽  
Author(s):  
W. F. Hickey ◽  
L. J. McMillan ◽  
T. J. McKearn ◽  
J. Gonatas ◽  
N. K. Gonatas

1983 ◽  
Vol 31 (9) ◽  
pp. 1126-1135 ◽  
Author(s):  
W F Hickey ◽  
V Lee ◽  
J Q Trojanowski ◽  
L J McMillan ◽  
T J McKearn ◽  
...  

Four monoclonal antibodies against guinea pig myelin basic protein (MBP), and four against subunits of bovine neurofilament triplet proteins (NF) were produced and their activity determined by enzyme-linked immunosorbant assay. The specificity and cross-reactivity of these eight monoclonal antibodies and one heterologous antiserum against each of the two central nervous system (CNS) antigens were examined in a histological study using the immunoperoxidase, antibody sandwich technique in rat and human brain tissue. Tissue sections were prepared from paraffin-embedded or fresh brain tissue that had been fixed with one of five different fixatives. The resulting immunoperoxidase labeling was then graded for intensity and examined for artifacts. One monoclonal antibody against MBP and one against NF resulted in labeling that was superior to that given by each of the antisera against their respective antigens. Of the five fixatives tested, a mercuric chloride-formalin solution gave the best preservation of these two antigens in rat and human brain tissue. The mercuric chloride-formalin solution was found to be superior to the other fixatives when immersion fixation was used, and was especially optimal when brains were perfused fixed. Three artifacts were encountered among the various antibody-fixative combinations that produced erroneous, but seemingly specific staining of Purkinje cells, neurons and axons, or astrocytes.


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