Purification of a recombinant membrane protein tagged with a calmodulin-binding domain: properties of chimeras of the Escherichia coli nicotinamide nucleotide transhydrogenase and the C-terminus of human plasma membrane Ca2+-ATPase

2004 ◽  
Vol 36 (1) ◽  
pp. 31-39 ◽  
Author(s):  
Maxim V Egorov ◽  
Anna Tigerström ◽  
Nikolay B Pestov ◽  
Tatyana V Korneenko ◽  
Maria B Kostina ◽  
...  
1989 ◽  
Vol 264 (21) ◽  
pp. 12313-12321 ◽  
Author(s):  
A Enyedi ◽  
T Vorherr ◽  
P James ◽  
D J McCormick ◽  
A G Filoteo ◽  
...  

Biochemistry ◽  
1990 ◽  
Vol 29 (2) ◽  
pp. 355-365 ◽  
Author(s):  
Thomas Vorherr ◽  
Peter James ◽  
Joachim Krebs ◽  
Agnes Enyedi ◽  
Daniel J. McCormick ◽  
...  

Metallomics ◽  
2015 ◽  
Vol 7 (9) ◽  
pp. 1319-1330 ◽  
Author(s):  
Elizabeth M. Bafaro ◽  
Sagar Antala ◽  
Tuong-Vi Nguyen ◽  
Stephen P. Dzul ◽  
Brian Doyon ◽  
...  

The human (h) ZIP4 transporter is a plasma membrane protein which functions to increase the cytosolic concentration of zinc.


1999 ◽  
Vol 274 (1) ◽  
pp. 527-531 ◽  
Author(s):  
Anil K. Verma ◽  
Katalin Paszty ◽  
Adelaida G. Filoteo ◽  
John T. Penniston ◽  
Agnes Enyedi

1992 ◽  
Vol 283 (2) ◽  
pp. 355-359 ◽  
Author(s):  
H P Adamo ◽  
J T Penniston

Alternative splices capable of generating proteins with altered functions were found (by PCR) in isoform 2 of the rat plasma membrane Ca2+ pump. These splices were concentrated in two hypervariable regions. One of these regions, near the N-terminus and the lipid-binding region, could be altered by the insertion of either or both of inserts x and y. Insertion of both x and y would add 45 amino acids to the molecule. The y insert causes the appearance of a rather hydrophobic stretch of amino acids in the middle of a highly polar region. The second variable region begins in the middle of the calmodulin-binding domain. Insertion of 229 nucleotides at this point of the message converts the b form to the a form, which has an altered (and shorter) C-terminus. The calmodulin-binding domain of this shortened form has a less basic character, which would decrease the affinity for calmodulin. The b form of isoenzyme 2 contains relatively weak protein kinase A substrate sequences, such as KQNSS and KNNS. These sequences are eliminated in form a, and a strongly activated kinase substrate sequence, RRQSS, appears in a different place. Different tissues use different combinations of alternative splices, with heart and brain showing the greatest diversity.


1996 ◽  
Vol 271 (7) ◽  
pp. 3714-3718 ◽  
Author(s):  
Anil K. Verma ◽  
Agnes Enyedi ◽  
Adelaida G. Filoteo ◽  
Emanuel E. Strehler ◽  
John T. Penniston

Sign in / Sign up

Export Citation Format

Share Document