Characterization of the purified membrane attachment (δ) subunit of the proton translocating adenosine triphosphatase from Escherichia coli

Biochemistry ◽  
1977 ◽  
Vol 16 (18) ◽  
pp. 4020-4025 ◽  
Author(s):  
Paul C. Sternweis ◽  
Jeffrey B. Smith
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphatase ◽  
Membrane Attachment

Characterization of the inhibitory (.epsilon.) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli

Biochemistry ◽  
1980 ◽  
Vol 19 (3) ◽  
pp. 526-531 ◽  
Author(s):  
Paul C. Sternweis ◽  
Jeffrey B. Smith
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphatase ◽  
Epsilon Subunit

scholarly journals Characterization of the mutant-unc D-gene product in a strain of Escherichia coli K12. An altered β-subunit of the magnesium ion-stimulated adenosine triphosphatase

1978 ◽  
Vol 172 (3) ◽  
pp. 523-531 ◽  
Author(s):  
D R H Fayle ◽  
J A Downie ◽  
G B Cox ◽  
F Gibson ◽  
J Radik
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphatase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Beta Subunit ◽  
Beta Subunits ◽  
Normal Strain ◽  
Diploid Strain ◽  
Escherichia Coli K12 ◽  
Low Ionic Strength

Membranes from a mutant strain of Escherichia coli K12 carrying the uncD409 allele were washed in low-ionic-strength buffers in the presence or absence of the proteinase inhibitor p-aminobenzamidine. Unlike membranes from a normal strain, those from strain AN463 (uncD409) did not become proton-permeable, as judged by NADH-induced atebrinfluorescence quenching, when the membranes were washed in the absence of p-aminobenzamide. Furthermore, ATP-dependent atebrin-fluorscence quenching in such washed membranes could not be reconstituted by the addition of solubilized Mg2+-stimulated adenosine triphosphatase preparations. The examination by two-dimensional polyacrylamide-gel electrophoresis of the polypeptide composition of the washed membranes from strain AN463 (uncD409) indicated the presence of a polypeptide of similar molecular weight to the normal beta-subunit of the Mg2+-stimulated adenosine triphosphatase, but with an altered isoelectric point. Both the normal and abnormal beta-subunits were identified in membranes prepared from a partial diploid strain carrying both the unc+ and uncD409 alleles. It is concluded that the uncD gene codes for the beta-subunit of the Mg2+-stimulated adenosine triphosphatase.

Purification of membrane attachment and inhibitory subunits of the proton translocating adenosine triphosphatase from Escherichia coli

Biochemistry ◽  
1977 ◽  
Vol 16 (2) ◽  
pp. 306-311 ◽  
Author(s):  
Jeffrey B. Smith ◽  
Paul C. Sternweis
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphatase ◽  
Membrane Attachment

Cloning and high level expression of Cynodon dactylon (Bermuda grass) pollen profilin (Cyn d 12) in Escherichia coli: purification and characterization of the allergen

1997 ◽  
Vol 27 (11) ◽  
pp. 1307-1313 ◽  
Author(s):  
J. A. ASTURIAS ◽  
M. C. ARILLA ◽  
N. GOMEZ-BAYON ◽  
J. MARTINEZ ◽  
A. MARTINEZ ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Grass Pollen ◽  
Cynodon Dactylon ◽  
Bermuda Grass ◽  
Purification And Characterization ◽  
High Level Expression ◽  
Bermuda Grass Pollen ◽  
D 12 ◽  
High Level
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