scholarly journals Distinctions between Hydrophobic Helices in Globular Proteins and Transmembrane Segments as Factors in Protein Sorting

2008 ◽  
Vol 284 (8) ◽  
pp. 5395-5402 ◽  
Author(s):  
Fiona Cunningham ◽  
Arianna Rath ◽  
Rachel M. Johnson ◽  
Charles M. Deber
Keyword(s):  
Protein Sorting ◽  
Globular Proteins ◽  
Transmembrane Segments ◽  
Hydrophobic Helices

Albumins as Embedding Media for Electron Microscopy

1969 ◽  
Vol 27 ◽  
pp. 422-423 ◽  
Author(s):  
J. L. Farrant ◽  
J. D. McLean
Keyword(s):  
Electron Microscopy ◽  
Electron Microscope ◽  
High Temperature ◽  
Biological Material ◽  
Globular Proteins ◽  
The Past ◽  
Antibody Staining ◽  
Thin Sectioning ◽  
Embedding Medium

For electron microscope techniques such as ferritin-labeled antibody staining it would be advantageous to have available a simple means of thin sectioning biological material without subjecting it to lipid solvents, impregnation with plastic monomers and their subsequent polymerization. With this aim in view we have re-examined the use of protein as an embedding medium. Gelatin which has been used in the past is not very satisfactory both because of its fibrous nature and the high temperature necessary to keep its solutions fluid. We have found that globular proteins such as the serum and egg albumins can be cross-linked so as to yield blocks which are suitable for ultrathin sectioning.

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