The requirement of ammonium or other cations linked with p-cresol sulfate for cross-reactivity with a peptide of myelin basic protein

2003 ◽  
Vol 418 (2) ◽  
pp. 119-124 ◽  
Author(s):  
Patricia L Jackson ◽  
Ligong Cao ◽  
J.Edwin Blalock ◽  
John N Whitaker
Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 316
Author(s):  
Svetlana V. Baranova ◽  
Pavel S. Dmitrenok ◽  
Valentina N. Buneva ◽  
Sergey E. Sedykh ◽  
Georgy A. Nevinsky

Histones play important roles in chromatin functioning and gene transcription, but in the intercellular space, they are harmful since they stimulate systemic inflammatory and toxic responses. Electrophoretically homogeneous IgGs against myelin basic protein (MBP), as well as H3 and H4 histones, were isolated from sera of HIV-infected patients. In contrast to known classical proteases, these IgGs split exclusively only histones and MBP but no other control proteins. Among 13 sites of hydrolysis of H3 by IgGs against H3 and 14 sites for anti-MBP IgGs, only two sites of the hydrolysis were the same. Between seven cleavage sites of H4 with IgGs against H4 and 9 sites of this histone hydrolysis by antibodies against MBP, only three sites were the same. The sites of hydrolysis of H3 (and H4) with abzymes against these histones and against MBP were different, but several expended protein clusters containing hydrolysis sites are partially overlapped. The existence of enzymatic cross-reactivity of abzymes against H3 and H4 and MBP represents a great menace to humans since due to cell apoptosis, histones constantly occur in human blood. They can hydrolyze MBP of the myelin sheath of axons and play a negative role in the pathogenesis of HIV-infected patients.


2002 ◽  
Vol 68 (2) ◽  
pp. 268-272 ◽  
Author(s):  
Mara Cirone ◽  
Laura Cuomo ◽  
Claudia Zompetta ◽  
Stefano Ruggieri ◽  
Luigi Frati ◽  
...  

1999 ◽  
Vol 194 (1) ◽  
pp. 118-123 ◽  
Author(s):  
Annette Pohl-Koppe ◽  
Eric L. Logigian ◽  
Allen C. Steere ◽  
David A. Hafler

1998 ◽  
Vol 89 (3) ◽  
pp. 304-311 ◽  
Author(s):  
Ahmad Al-Sabbagh ◽  
Celia A.A.C. Garcia ◽  
Blanca M. Diaz-Bardales ◽  
Cristiane Zaccarias ◽  
Julia Keiko Sakurada ◽  
...  

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.


1984 ◽  
Vol 9 (9) ◽  
pp. 1295-1308 ◽  
Author(s):  
Kenneth J. Lazarus ◽  
George A. Hashim ◽  
Philip Y. Paterson ◽  
Eugene D. Day

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