scholarly journals Cysteine-based crosslinking approach for characterization of oligomeric pore-forming proteins in the mitochondrial membranes

2021 ◽  
Author(s):  
Zhi Zhang ◽  
Bo Huang ◽  
Xuejun C. Zhang ◽  
Jialing Lin
Keyword(s):  
Mitochondrial Membranes ◽  
Pore Forming Proteins

scholarly journals Characterization of the binding of purified human C1q to heart mitochondrial membranes.

1981 ◽  
Vol 256 (21) ◽  
pp. 10924-10929
Author(s):  
S.B. Storrs ◽  
W.P. Kolb ◽  
R.N. Pinckard ◽  
M.S. Olson
Keyword(s):  
Mitochondrial Membranes

scholarly journals Purification and Characterization of the Voltage-Dependent Anion-Selective Channel Protein from Wheat Mitochondrial Membranes

1993 ◽  
Vol 101 (2) ◽  
pp. 579-587 ◽  
Author(s):  
A. Blumenthal ◽  
K. Kahn ◽  
O. Beja ◽  
E. Galun ◽  
M. Colombini ◽  
...  
Keyword(s):  
Mitochondrial Membranes ◽  
Purification And Characterization ◽  
Channel Protein ◽  
Voltage Dependent ◽  
Selective Channel

scholarly journals CHARACTERIZATION OF RAT LIVER SUBCELLULAR MEMBRANES

1974 ◽  
Vol 60 (2) ◽  
pp. 460-472 ◽  
Author(s):  
David H. DeHeer ◽  
Merle S. Olson ◽  
R. Neal Pinckard
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Nuclear Membrane ◽  
Membrane Fraction ◽  
Cross Reactivity ◽  
Selective Absorption ◽  
Mitochondrial Membranes ◽  
Subcellular Membrane ◽  
Hepatocellular Necrosis

The induction of acute hepatocellular necrosis in rats resulted in the production of complement fixing, IgM autoantibodies directed toward inner and outer mitochondrial membranes, microsomal membrane, lysosomal membrane, nuclear membrane, cytosol, but not to plasma membrane. Utilizing selective absorption procedures it was demonstrated that each subcellular membrane fraction possessed unique autoantigenic activity with little or no cross-reactivity between the various membrane fractions. It is proposed that the development of membrane-specific autoantibodies may provide an immunological marker useful in the differential characterization of various subcellular membranes.

scholarly journals Further characterization of agmatine binding to mitochondrial membranes: involvement of imidazoline I2 receptor

Amino Acids ◽  
2011 ◽  
Vol 42 (2-3) ◽  
pp. 761-768 ◽  
Author(s):  
Pamela Martinis ◽  
Valentina Battaglia ◽  
Silvia Grancara ◽  
Lisa Dalla Via ◽  
Vito Di Noto ◽  
...  
Keyword(s):  
Mitochondrial Membranes ◽  
Imidazoline I2 Receptor

scholarly journals Characterization of two monoclonal antibodies obtained after immunization with human liver mitochondrial membrane preparations

1984 ◽  
Vol 221 (3) ◽  
pp. 765-776 ◽  
Author(s):  
E E Billett ◽  
B Gunn ◽  
R J Mayer
Keyword(s):  
Monoclonal Antibodies ◽  
Human Liver ◽  
Portal Tract ◽  
Immunoperoxidase Staining ◽  
Cell Type ◽  
Spleen Cells ◽  
Mitochondrial Membranes ◽  
Particulate Distribution ◽  
Mouse Myeloma

Two monoclonal antibodies have been generated by fusion of mouse myeloma cells with spleen cells from mice immunized with human liver mitochondrial membranes. One antibody, 1H6/C12, an immunoglobulin G2a (IgG2a), binds to the inner membrane of rat hepatocyte mitochondria, and immunoperoxidase staining demonstrates that its epitope has an intracellular particulate distribution within rat and human hepatocytes and human brain neurons. The epitope reactive with 1H6/C12 is partially sensitive to proteinase digestion. The second antibody, 3F12/F2, an IgG1, binds to a contaminating cell type, namely the granulocyte, but it does not bind to monocytes, lymphocytes and red cells in human blood. This antibody reacts with cells in the portal tract and sinusoids of rat and human liver, as shown by immunoperoxidase staining. The epitope for 3F12/F2 is extremely sensitive to proteinase digestion and is only exposed when granulocytes are fixed in acetone, indicating an internal localization.

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