Elemental and molecular mass spectrometry for integrated selenosugar speciation in liver and kidney tissues of maternal feeding and supplemented rats

2015 ◽  
Vol 30 (1) ◽  
pp. 267-276 ◽  
Author(s):  
Héctor González-Iglesias ◽  
María Luisa Fernández-Sánchez ◽  
Ying Lu ◽  
Sonia Fernández Menéndez ◽  
Spiros A. Pergantis ◽  
...  

The integrated use of elemental and molecular ion sources for enhanced selenium speciation data in rat liver and kidneys, along with its potential for Se-supplement studies are highlighted.

1991 ◽  
Vol 278 (1) ◽  
pp. 171-177 ◽  
Author(s):  
A J Rivett ◽  
S T Sweeney

The multicatalytic proteinase (MCP) is a high-molecular-mass non-lysosomal proteinase that gives rise to a characteristic pattern of bands of molecular mass 22-34 kDa on SDS/PAGE gels. Isoelectric-focusing gels of the enzyme purified from rat liver show 16 bands with isoelectric points in the range of pH 5-8.5. Two-dimensional PAGE gels reveal that there are more than the previously reported 13 polypeptides associated with the MCP from rat liver and show a pattern of 15-20 major spots and several minor ones, similar to that of MCP isolated from some other sources. Possible relationships between the different polypeptides were investigated by immunoblot analysis of electrophoretically purified proteinase subunits with affinity-purified subunit-specific antibodies as well as antibodies raised against individual denatured subunits of the complex. The results demonstrate that many of the major polypeptide components of the MCP complex are antigenically distinct. Moreover comparison of immunoreactive material in crude cell extracts with that in purified MCP preparations has shown that the polypeptides are not derived from a smaller number of higher-molecular-mass subunits. Also, individual subunits have the same apparent molecular mass in a variety of rat tissues, suggesting close similarity between MCPs of different tissues. The highest concentrations of MCP subunits occur in liver and kidney. Gel-filtration analysis of crude extracts has demonstrated that MCP polypeptides are also associated with a higher-molecular-mass complex, which may be the 26 S proteinase that has been implicated in the degradation of ubiquitin-protein conjugates.


1978 ◽  
Vol 14 (9) ◽  
pp. 699-702
Author(s):  
L. N. Sosulina ◽  
L. I. Nazarova ◽  
E. M. Nikonorov ◽  
T. G. Zubkevich

2014 ◽  
Vol 406 (24) ◽  
pp. 5853-5865 ◽  
Author(s):  
Miguel Ángel García-Sevillano ◽  
Tamara García-Barrera ◽  
Francisco Navarro ◽  
Jürgen Gailer ◽  
José Luiz Gómez-Ariza

2008 ◽  
Vol 23 (3) ◽  
pp. 378-384 ◽  
Author(s):  
Diego Esteban-Fernández ◽  
M. Montes-Bayón ◽  
E. Blanco González ◽  
M. M. Gómez Gómez ◽  
M. A. Palacios ◽  
...  

2016 ◽  
Vol 88 (10) ◽  
pp. 5258-5263 ◽  
Author(s):  
Ann-Christin Niehoff ◽  
Jacqueline Schulz ◽  
Jens Soltwisch ◽  
Sören Meyer ◽  
Hans Kettling ◽  
...  

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