scholarly journals Impact of naturally occurring serine/cysteine variations on the structure and function of Pseudomonas metallothioneins

Metallomics ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 23-33 ◽  
Author(s):  
Jelena Habjanič ◽  
Serge Chesnov ◽  
Oliver Zerbe ◽  
Eva Freisinger

Naturally occurring Ser/Cys variations in Pseudomonas metallothioneinss affect intra-cluster dynamics rather than binding capacity.

IUBMB Life ◽  
2012 ◽  
Vol 64 (4) ◽  
pp. 346-353 ◽  
Author(s):  
Alexander Vargas-Hernández ◽  
Gabriela López-Herrera ◽  
José L. Maravillas-Montero ◽  
Felipe Vences-Catalán ◽  
Dolores Mogica-Martínez ◽  
...  

Blood ◽  
1983 ◽  
Vol 62 (1) ◽  
pp. 133-140 ◽  
Author(s):  
MP Croissant ◽  
M Zuzel ◽  
JP Allain

The interference of antibodies to factor VIII coagulant protein (VIII:C) of 9 nonhemophilic patients with the binding to factor VIII coagulant antigen (VIII:CAg) of a reference hemophilic 125I-Fab' reagent, used in a liquid phase VIII:CAg assay, was studied. The binding competition was estimated from immunoradiometric assay (IRMA) dose-response slope of VIII:CAg present in patient plasma, interference of antibodies with the 125I-Fab' binding to VIII:CAg in normal plasma, and the displacement of antibody from the complexes with VIII:CAg by the 125I Fab'. Antibody populations from three patients were studied in detail; in the VIII:CAg assay, two of them interfered with the 125I- Fab' binding, and one did not (patient 1). The formation of stable complexes between antibodies of each patient and VIII:CAg was demonstrated by protein-A-Sepharose adsorption. The 125I-Fab' binding to VIII:CAg-anti-VIII:CAg IgG complexes indicated that patient 1 antibodies and the 125I-Fab' recognized different antigenic determinants, whereas the other two patient antibodies and 125I-Fab' recognized closely related or identical VIII:CAg determinants. These results demonstrate an apparently selective recognition of at least two distinct VIII:CAg determinants by naturally occurring antibodies, suggesting a possibility of a wider use of these antibodies in studies of the structure and function of factor VIII.


2014 ◽  
Vol 28 (7) ◽  
pp. 1026-1038 ◽  
Author(s):  
Tsung-Sheng Wu ◽  
Geoffrey L. Hammond

2002 ◽  
Vol 30 (6) ◽  
pp. 1122-1126 ◽  
Author(s):  
R. A. Collins

Presented is a review of the discovery and characterization of the Neurospora Varkud satellite ribozyme. It outlines the approaches and observations that have led to our current level of understanding of the structure and function of this ribozyme, and highlights its distinctive features compared with other naturally occurring small ribozymes.


Blood ◽  
1983 ◽  
Vol 62 (1) ◽  
pp. 133-140
Author(s):  
MP Croissant ◽  
M Zuzel ◽  
JP Allain

Abstract The interference of antibodies to factor VIII coagulant protein (VIII:C) of 9 nonhemophilic patients with the binding to factor VIII coagulant antigen (VIII:CAg) of a reference hemophilic 125I-Fab' reagent, used in a liquid phase VIII:CAg assay, was studied. The binding competition was estimated from immunoradiometric assay (IRMA) dose-response slope of VIII:CAg present in patient plasma, interference of antibodies with the 125I-Fab' binding to VIII:CAg in normal plasma, and the displacement of antibody from the complexes with VIII:CAg by the 125I Fab'. Antibody populations from three patients were studied in detail; in the VIII:CAg assay, two of them interfered with the 125I- Fab' binding, and one did not (patient 1). The formation of stable complexes between antibodies of each patient and VIII:CAg was demonstrated by protein-A-Sepharose adsorption. The 125I-Fab' binding to VIII:CAg-anti-VIII:CAg IgG complexes indicated that patient 1 antibodies and the 125I-Fab' recognized different antigenic determinants, whereas the other two patient antibodies and 125I-Fab' recognized closely related or identical VIII:CAg determinants. These results demonstrate an apparently selective recognition of at least two distinct VIII:CAg determinants by naturally occurring antibodies, suggesting a possibility of a wider use of these antibodies in studies of the structure and function of factor VIII.


1995 ◽  
Vol 309 (3) ◽  
pp. 787-791 ◽  
Author(s):  
S Clément ◽  
J G Delcros ◽  
H S Basu ◽  
G Quash ◽  
L J Marton ◽  
...  

The naturally occurring polyamine spermine induces haemoglobin synthesis in murine erythroleukaemia (MEL) cells. We have studied the ability of various polyamine analogues to inhibit cell growth and induce haemoglobin production. Polyamine analogues with free terminal amino groups were good inducers of haemoglobin production in MEL cells. Haemoglobin levels correlated with the number of positive charges: pentamines (five positive charges) were stronger inducers than tetramines (four positive charges). Compounds ethylated at their terminal amines were poor inducers of haemoglobin production but good inhibitors of MEL cell growth. These results provide evidence that polyamine analogues support specific biological functions of polyamines in MEL cells and suggest relationships between polyamine structure and function.


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