Determination of molecular weights of plant viral protein subunits by polyacrylamide gel electrophoresis

Virology ◽  
1970 ◽  
Vol 42 (3) ◽  
pp. 724-731 ◽  
Author(s):  
J.A. Lesnaw ◽  
M.E. Reichmann
Keyword(s):  
Viral Protein ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Protein Subunits ◽  
Molecular Weights

COMPARISON OF GLIADIN AND GLUTENIN SUBUNITS IN THE TRITICINAE BY SDS-POLYACRYLAMIDE GEL ELECTROPHORESIS

1975 ◽  
Vol 55 (3) ◽  
pp. 667-672 ◽  
Author(s):  
K. R. PRESTON ◽  
W. WOODBURY ◽  
R. A. ORTH ◽  
W. BUSHUK
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Triticum Aestivum L ◽  
Polyacrylamide Gel ◽  
Glutenin Subunits ◽  
Protein Subunits ◽  
Molecular Weights ◽  
Aegilops Squarrosa ◽  
Secale Cereale L

Protein subunits obtained by reduction of gliadin and glutenin from Triticum aestivum L. em. Thell. (AABBDD), Triticum monococcum L. (AA), Aegilops squarrosa L. (DD) and Secale cereale L. (RR) were examined by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. Seven of the twelve gliadin subunits and nine of the fifteen glutenin subunits present in T. aestivum had molecular weights (MW’s) similar to subunits present in both T. monococcum and A. squarrosa. An additional five gliadin and five glutenin subunits present in T. aestivum had MW’s similar to subunits present in T. monococcum or A. squarrosa. S. cereale had a lower number of gliadin and glutenin subunits. However, three of four gliadin subunits and eight of nine glutenin subunits had MW’s similar to subunits present in the Triticum–Aegilops groups. These results have been used to consider evolutionary relationships in the Triticinae.

Platelet Microtubule Subunit Proteins

1979 ◽  
Vol 42 (05) ◽  
pp. 1630-1633 ◽  
Author(s):  
A G Castle ◽  
N Crawford
Keyword(s):  
Epithelial Cells ◽  
Gel Electrophoresis ◽  
Blood Platelets ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Lens Epithelial Cells ◽  
Molecular Weights ◽  
Kinetics Of ◽  
Microtubular Structures

SummaryBlood platelets contain microtubule proteins (tubulin and HMWs) which can be polymerised “in vitro” to form structures which resemble the microtubules seen in the intact platelet. Platelet tubulin is composed of two non-identical subunits a and p tubulin which have molecular weights around 55,000 but can be resolved in alkaline SDS-polyacrylamide gel electrophoresis. These subunits associate as dimers with sedimentation coefficients of about 5.7 S although it is not known whether the dimer protein is a homo- or hetero-dimer. The dimer tubulin binds the anti-mitotic drug colchicine and the kinetics of this binding are similar to those reported for neurotubulins. Platelet microtubules also contain two HMW proteins which appear to be essential and integral components of the fully assembled microtubule. These proteins have molecular weights greater than 200,000 daltons. Fluorescent labelled antibodies to platelet and brain tubulins stain long filamentous microtubular structures in bovine lens epithelial cells and this pattern of staining is prevented by exposing the cells to conditions known to cause depolymerisation of cell microtubules.

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