Identification of a 283-kDa Protein Component of the Particulate Matrix Associated with Cardiac Mesenchyme Formation

1996 ◽  
Vol 155 (4) ◽  
pp. 219-230 ◽  
Author(s):  
A.R. Sinning ◽  
C.C. Hewitt
2013 ◽  
Vol 198 (5) ◽  
pp. 338-348 ◽  
Author(s):  
Tarek Hamdy Abd-Elhamid ◽  
Marianne L. Conway ◽  
Allan R. Sinning

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Tarek Hamdy Abd‐Elhamid ◽  
Marianne L. Conway ◽  
Allan R Sinning

Author(s):  
J. T. Stasny ◽  
R. C. Burns ◽  
R. W. F. Hardy

Structure-functlon studies of biological N2-fixation have correlated the presence of the enzyme nitrogenase with increased numbers of intracytoplasmic membranes in Azotobacter. However no direct evidence has been provided for the internal cellular localization of any nitrogenase. Recent advances concerned with the crystallizatiorTand the electron microscopic characterization of the Mo-Fe protein component of Azotobacter nitrogenase, prompted the use of this purified protein to obtain antibodies (Ab) to be conjugated to electron dense markers for the intracellular localization of the protein by electron microscopy. The present study describes the use of ferritin conjugated to goat antitMo-Fe protein immunoglobulin (IgG) and the observations following its topical application to thin sections of N2-grown Azotobacter.


Author(s):  
R. M. Simonyan ◽  
K. V. Simonyan ◽  
S. M. Feschyan ◽  
V. A. Chavushyan ◽  
G. M. Simonyan ◽  
...  

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