scholarly journals The characterization of an acidic calmodulin-binding protein in brain cytoskeleton and membrane fractions

1986 ◽  
Vol 240 (2) ◽  
pp. 593-596
Author(s):  
P Strocchi ◽  
J M Gilbert
Keyword(s):  
Intermediate Filament ◽  
Gel Electrophoresis ◽  
Binding Protein ◽  
Two Dimensional ◽  
Proteolytic Digestion ◽  
Two Dimensional Gel Electrophoresis ◽  
Intermediate Filament Proteins ◽  
Calmodulin Binding ◽  
Acidic Proteins

One of the most abundant acidic proteins in rat brain has an Mr of 68,000 and a pI of 5.6 (68K 5.6 protein) when analysed by two-dimensional gel electrophoresis. The 68K 5.6 protein was found in large relative amounts in brain cytoskeleton preparations and in membrane and supernatant fractions. High-salt washing and proteolytic digestion did not remove this protein from the membrane elements. The 68K 5.6 protein was also found in the microtubule-associated protein fraction of purified microtubules and was present in large relative amounts in preparations of intermediate-filament proteins. The 68K 5.6 protein binds to calmodulin in the presence of Ca2+ ions, and we found it to be an abundant acidic calmodulin-binding protein in brain tissue.

scholarly journals Cholera toxin can catalyze ADP-ribosylation of cytoskeletal proteins.

1981 ◽  
Vol 91 (2) ◽  
pp. 410-413 ◽  
Author(s):  
H R Kaslow ◽  
V E Groppi ◽  
M E Abood ◽  
H R Bourne
Keyword(s):  
Adenylate Cyclase ◽  
Cholera Toxin ◽  
Intermediate Filament ◽  
Gel Electrophoresis ◽  
Cytoskeletal Proteins ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Intermediate Filament Proteins ◽  
Adp Ribosylation ◽  
Human Foreskin Fibroblasts

Cholera toxin catalyzes transfer of radiolabel from [32P]NAD+ to several peptides in particulate preparations of human foreskin fibroblasts. Resolution of these peptides by two-dimensional gel electrophoresis allowed identification of two peptides of Mr = 42,000 and 52,000 as peptide subunits of a regulatory component of adenylate cyclase. The radiolabeling of another group of peptides (Mr = 50,000 to 65,000) suggested that cholera toxin could catalyze ADP-ribosylation of cytoskeletal proteins. This suggestion was confirmed by showing that incubation with cholera toxin and [32P]NAD+ caused radiolabeling of purified microtubule and intermediate filament proteins.

Characterization of antithrombin III from human plasma by two-dimensional gel electrophoresis and capillary electrophoretic methods

2003 ◽  
Vol 24 (24) ◽  
pp. 4282-4290 ◽  
Author(s):  
Leopold Kremser ◽  
Andrea Brückner ◽  
Andrea Heger ◽  
Tom Grunert ◽  
Andrea Buchacher ◽  
...  
Keyword(s):  
Human Plasma ◽  
Gel Electrophoresis ◽  
Antithrombin Iii ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Capillary Electrophoretic

Characterization of Enterobacter cloacae under phoxim stress by two-dimensional gel electrophoresis

2015 ◽  
Vol 20 (3) ◽  
pp. 403-409 ◽  
Author(s):  
Dijun Zhang ◽  
Jiajie Xu ◽  
Weina He ◽  
Qianqian Tong ◽  
Liping Chen ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Enterobacter Cloacae ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis
Sign in / Sign up

Export Citation Format

Share Document