Identification and biochemical characterization of the plasma-membrane H+-ATPase in guard cells of Vicia faba L.

Planta ◽  
1993 ◽  
Vol 190 (1) ◽  
Author(s):  
Dirk Becker ◽  
Carsten Zeilinger ◽  
Gabi Lohse ◽  
Hans Depta ◽  
Rainer Hedrich
1995 ◽  
Vol 36 (5) ◽  
pp. 919-924 ◽  
Author(s):  
Nobuyoshi Nakajima ◽  
Hikaru Saji ◽  
Mitsuko Aono ◽  
Noriaki Kondo

Planta ◽  
1992 ◽  
Vol 188 (2) ◽  
pp. 206-214 ◽  
Author(s):  
Gabi Lohse ◽  
Rainer Hedrich

Planta ◽  
1990 ◽  
Vol 181 (3) ◽  
Author(s):  
H.M. Brindley
Keyword(s):  

2001 ◽  
Vol 7 (S2) ◽  
pp. 1030-1031
Author(s):  
J.M. Robinson

There are three members of the caveolin (CAV) gene family that give rise to four polypeptides. These polypeptides are CAV-1α, CAV-1β, CAV-2, and CAV-3. The CAV-1β isoform is a truncated form of CAV-1α that lacks 31 amino acids at the N-terminus of the molecule. The CAV- 1β molecule arises through an alternative splicing mechanism.Caveolae are specialized plasma membrane microdomains that are expressed at high levels in some cell types (e.g., endothelium, adipocytes, fibroblasts). These specialized regions of the plasma membrane have a characteristic omega-shaped appearance with diameters ranging from 40-90 run. They are distinct from clathrin-coated pits since they lack the characteristic coated appearance in electron microscopy. Caveolae were among the first structures to be discovered by biological electron microscopy. However, biochemical characterization of these structures did not begin in earnest until a marker protein was identified. The initial marker was the 22-kDa protein known as caveolin.


1977 ◽  
Vol 107 (7) ◽  
pp. 1313-1324 ◽  
Author(s):  
Ronald R. Marquardt ◽  
A. Thomas Ward ◽  
Lloyd D. Campbell ◽  
Peter E. Cansfield

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