scholarly journals Detection of low molecular mass GTP-binding proteins in chromaffin granules and other subcellular fractions of chromaffin cells

FEBS Letters ◽  
1989 ◽  
Vol 247 (1) ◽  
pp. 127-131 ◽  
Author(s):  
Jean-Pierre Doucet ◽  
Susan Fournier ◽  
Manohar Parulekar ◽  
José-María Trifaró
Keyword(s):  
Molecular Mass ◽  
Chromaffin Cells ◽  
Binding Proteins ◽  
Subcellular Fractions ◽  
Chromaffin Granules ◽  
Gtp Binding Proteins ◽  
Gtp Binding

scholarly journals Identification of the ral and rac1 Gene Products, Low Molecular Mass GTP-binding Proteins from Human Platelets

1989 ◽  
Vol 264 (28) ◽  
pp. 16383-16389
Author(s):  
P G Polakis ◽  
R F Weber ◽  
B Nevins ◽  
J R Didsbury ◽  
T Evans ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Binding Proteins ◽  
Human Platelets ◽  
Gene Products ◽  
Gtp Binding Proteins ◽  
Gtp Binding

Bacterial protein toxins inhibiting low-molecular-mass GTP-binding proteins

2001 ◽  
Vol 291 (4) ◽  
pp. 243-250 ◽  
Author(s):  
Ingo Just ◽  
Fred Hofmann ◽  
Harald Genth ◽  
Ralf Gerhard
Keyword(s):  
Molecular Mass ◽  
Binding Proteins ◽  
Bacterial Protein ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Protein Toxins

scholarly journals Purification and N-terminal sequence of the p21rho GTPase-activating protein, rho GAP

1991 ◽  
Vol 276 (3) ◽  
pp. 833-836 ◽  
Author(s):  
M D Garrett ◽  
G N Major ◽  
N Totty ◽  
A Hall
Keyword(s):  
Molecular Mass ◽  
Binding Proteins ◽  
Enzymic Activity ◽  
Gtpase Activity ◽  
Ras Proteins ◽  
Terminal Sequence ◽  
Human Spleen ◽  
Gtp Binding Proteins ◽  
Gtpase Activating Proteins ◽  
Gtp Binding

Eukaryotic cells contain numerous small-molecular-mass GTP-binding proteins, but the processes that they regulate are not known. Different members of this protein family appear to be associated with specific GTPase-activating proteins (GAPs), and we have previously reported the identification of a cytoplasmic GAP (rho GAP) that stimulates the GTPase activity of p21rho but not of other small-molecular-mass GTP-binding proteins. We have now purified rho GAP 2000-fold from human spleen tissue using f.p.l.c. Electrotransfer of this 27.5 kDa protein on to an Immobilon-P transfer membrane followed by reconstitution of its enzymic activity confirmed its identity. Rho GAP was subjected to N-terminal sequence analysis and 15 amino acids were obtained. The sequence showed 53% identity with a region present in IRA1, a protein which stimulates the GTPase activity of RAS proteins in Saccharomyces cerevisiae. These results suggest that there is a family of sequence-related GAP proteins, which to date includes ras GAP and its yeast counterparts IRA1 and IRA2, rho GAP and the Neurofibromatosis gene product NF1.

scholarly journals Distribution of polypeptides binding guanosine 5′-[γ-[35S]thio]triphosphate and anti-(ras protein) antibodies in liver subcellular fractions. Evidence for endosome-specific components

1990 ◽  
Vol 271 (1) ◽  
pp. 179-183 ◽  
Author(s):  
N Ali ◽  
W H Evans
Keyword(s):  
Rat Liver ◽  
Subcellular Distribution ◽  
Plasma Membranes ◽  
Binding Proteins ◽  
Subcellular Fractions ◽  
Relative Distribution ◽  
Ras Proteins ◽  
Ras Protein ◽  
Gtp Binding Proteins ◽  
Gtp Binding

The subcellular distribution in rat liver of polypeptides binding guanosine 5′-[gamma-[35S]thio]triphosphate [( 35S]GTP[S]) and seven antibodies against ras oncoproteins was evaluated. Multiple low-Mr (21,000-28,000) GTP-binding proteins were detected, but their relative distribution among the membrane fractions varied. A more specific compartmentation of polypeptides which bind antibodies generated against ras proteins was evident, with an Mr-28,000 polypeptide and a probable Mr-56,000 dimer, identified by six of the antibodies tested, being confined mainly to endosomes. An Mr-23,000 polypeptide was detected by some of the antibodies in all of the membrane fractions, but especially in the plasma membranes.

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