scholarly journals Purification, Characterization, and Partial Amino Acid Sequence of a G Protein-activated Phospholipase C from Squid Photoreceptors

1995 ◽  
Vol 270 (2) ◽  
pp. 854-859 ◽  
Author(s):  
Jane Mitchell ◽  
Joanne Gutierrez ◽  
John K. Northup
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase C ◽  
G Protein ◽  
Partial Amino Acid Sequence

scholarly journals Identification of Gα11 as the phospholipase C-activating G-protein of turkey erythrocytes

1993 ◽  
Vol 290 (3) ◽  
pp. 765-770 ◽  
Author(s):  
D H Maurice ◽  
G L Waldo ◽  
A J Morris ◽  
R A Nicholas ◽  
T K Harden
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase C ◽  
G Protein ◽  
Expression System ◽  
Cdna Libraries ◽  
Dependent Manner ◽  
Alpha Subunits ◽  
G Protein Alpha Subunit ◽  
G Alpha Q

A 43 kDa phospholipase C-activating protein has been purified previously from turkey erythrocytes and shown to express immunological properties expected of that of the Gq family of G-protein alpha-subunits [Waldo, Boyer, Morris and Harden (1991) J. Biol. Chem. 266, 14217-14225]. Internal amino acid sequence has now been obtained from this protein which shares 50-100% sequence identity with sequences encoded by mammalian G alpha 11 and G alpha q cDNAs. To identify the purified protein unambiguously, it was necessary to compare its amino acid sequence with the sequence encoded by avian G-protein alpha-subunit cDNA. As such, mouse G alpha q was used as a probe to screen turkey brain and fetal-turkey blood cDNA libraries. A full-length cDNA was identified that encodes avian G alpha 11, on the basis of its 96-98% amino acid identity with mammalian G alpha 11. All eight peptides sequenced from the turkey erythrocyte phospholipase C-activating protein are completely contained within the deduced amino acid sequence of the avian G alpha 11 cDNA. Expression of this cDNA in Sf9 cells by using a baculovirus expression system resulted in the production of a 43 kDa protein that reacts strongly with antisera to the Gq family of G-protein alpha-subunits and activated purified avian phospholipase C in an AlF4(-)-dependent manner. Taken together, these results unambiguously identify the protein purified from turkey erythrocytes, on the basis of its capacity to activate avian phospholipase C, as G alpha 11.

Partial Amino Acid Sequence of a Cellulase-Like Component with IgE-Binding Properties from Stachybotrys chartarum

2004 ◽  
Vol 133 (2) ◽  
pp. 136-144 ◽  
Author(s):  
Marja Kärkkäinen ◽  
Päivi Raunio ◽  
Jaakko Rautiainen ◽  
Seppo Auriola ◽  
Kaj Hinke ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Stachybotrys Chartarum ◽  
Partial Amino Acid Sequence ◽  
Binding Properties ◽  
Ige Binding

SOME ASPECTS OF THE STRUCTURE OF HEMOGLOBIN

1964 ◽  
Vol 42 (6) ◽  
pp. 755-762 ◽  
Author(s):  
David B. Smith
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Partial Amino Acid Sequence ◽  
Heme Pocket ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Kinetics Of ◽  
Β Chain

An outline of present ideas concerning the arrangement, folding, and chemistry of the polypeptide chains of hemoglobin is given with some references to present know ledge of myoglobin.New material includes a partial amino acid sequence of the β-chain of horse hemoglobin, details concerning the amino acids lining the heme pocket of horse hemoglobin, and the effects of carboxypeptidases A and B on horse oxy- and horse deoxy-hemoglobin. The kinetics of the latter reactions are not simple. The C-terminal amino acids are released more rapidly from the oxygenated form.

scholarly journals Purification and partial amino acid sequence of a mu opioid receptor from rat brain.

1993 ◽  
Vol 268 (35) ◽  
pp. 26447-26451
Author(s):  
C M Eppler ◽  
J D Hulmes ◽  
J B Wang ◽  
B Johnson ◽  
M Corbett ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rat Brain ◽  
Opioid Receptor ◽  
Mu Opioid Receptor ◽  
Partial Amino Acid Sequence ◽  
Mu Opioid
Sign in / Sign up

Export Citation Format

Share Document