[14] Purification of EEA1 from bovine brain cytosol using Rab5 affinity chromatography and activity assays

Author(s):  
Savvas Christoforidis ◽  
Marino Zerial
1989 ◽  
Vol 165 (1) ◽  
pp. 284-291 ◽  
Author(s):  
Harald H.H.W. Schmidt ◽  
Petra Wilke ◽  
Birgit Evers ◽  
Eycke Böhme

1984 ◽  
Vol 220 (1) ◽  
pp. 291-299 ◽  
Author(s):  
T Kealey ◽  
P J Randle

Actomyosin was partially purified from rat parotid cells dispersed by collagenase digestion and found to possess different solubility characteristics from that from (undispersed) rat parotid tissue. This is attributed to the decrease in vascular contamination effected by the isolation of parotid cells, yielding a non-muscle actomyosin [Adelstein, Conti, Johnson, Pastan & Pollard (1972) Proc. Natl. Acad. Sci. U.S.A. 69, 3693-3697]. Myosin light-chain kinase was partially purified from dispersed rat parotid cells by calmodulin affinity chromatography and shown to be activated by Ca2+-calmodulin. The calmodulin content of dispersed rat parotid cells was shown to be 6.50 +/- 0.59 ng of calmodulin/micrograms of rat parotid-cell protein (mean +/- S.E.M.), as determined by the activation of purified bovine brain phosphodiesterase by heat-treated extracts of dispersed rat parotid cells.


1989 ◽  
Vol 49 ◽  
pp. 276
Author(s):  
Satoshi Matsushima ◽  
Akitoshi Kato ◽  
Kaname Nakatani ◽  
Shiro Waga ◽  
Toshio Tanaka

1990 ◽  
Vol 169 (2) ◽  
pp. 652-659 ◽  
Author(s):  
Mitsuo Isomura ◽  
Kozo Kaibuchi ◽  
Takeshi Yamamoto ◽  
Shiro Kawamura ◽  
Masaya Katayama ◽  
...  

1996 ◽  
Vol 271 (41) ◽  
pp. 25213-25219 ◽  
Author(s):  
Jae Ho Kim ◽  
Yoon Jung Suh ◽  
Taehoon G. Lee ◽  
Yong Kim ◽  
Sun Sik Bae ◽  
...  

1987 ◽  
Vol 166 (2) ◽  
pp. 333-338 ◽  
Author(s):  
Francoise SCHOENTGEN ◽  
Florence SACCOCCIO ◽  
Jacqueline JOLLES ◽  
Ida BERNIER ◽  
Pierre JOLLES

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