scholarly journals A 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties

1988 ◽  
Vol 251 (3) ◽  
pp. 777-785 ◽  
Author(s):  
F Martin ◽  
J Derancourt ◽  
J P Capony ◽  
A Watrin ◽  
J C Cavadore
Keyword(s):  
Plasma Membrane ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein Complex ◽  
Actin Filaments ◽  
Thin Filament ◽  
Partial Amino Acid Sequence ◽  
Calmodulin Binding

Interaction of plasma membrane with the cytoskeleton involves a large number of proteins, among them a 36 kDa protein that was found to be involved in the interaction with actin filaments. We have isolated a 36 kDa protein from bovine aorta as a monomer and in a complex with a 10 kDa protein. Partial amino acid sequence determinations show that the 36 kDa and 10 kDa proteins isolated from bovine aorta are analogous to or identical with corresponding proteins purified from bovine intestine already described by Kristensen, Saris, Hunter, Hicks, Noonan, Glenney & Tack [(1986) Biochemistry 25, 4497-4503]. We report here that the association of the 10 kDa protein with the 36 kDa protein confers specific calmodulin-binding and actin-severing properties on the complex that are not possessed by the 36 kDa monomer alone. These findings suggest that the protein complex could be involved in thin-filament-related structures or could modulate some Ca2+-regulated events mediated by calmodulin.

scholarly journals The binding of calmodulin to myelin basic protein and histone H2B

1980 ◽  
Vol 189 (2) ◽  
pp. 227-240 ◽  
Author(s):  
R J Grand ◽  
S V Perry
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Binding Protein ◽  
Bovine Brain ◽  
Sequence Determination ◽  
Partial Amino Acid Sequence ◽  
Histone H2b ◽  
Calmodulin Binding

1. A calmodulin-binding protein of apparent mol.wt. 19 000 has been purified from chicken gizzard. Similar proteins have been isolated from bovine uterus, rabbit skeletal muscle and rabbit liver. 2. These proteins migrated as an equimolar complex with bovine brain calmodulin on electroporesis on polyacrylamide gels in the presence of Ca2+ and 6M-urea. The complex was dissociated in the presence of EGTA. 2. The chicken gizzard calmodulin-binding protein has been shown to be identical with chicken erythrocyte histone H2B on the basis of partial amino acid sequence determination. 4. The calmodulin-binding proteins of apparent mol.wt. 22 000 isolated previously from bovine brain [Grand & Perry (1979) Biochem. J. 183, 285-295] has been shown, on the basis of partial amino-acid-sequence determination, to be identical with myelin basic protein. 5. The activation of bovine brain phosphodiesterase by calmodulin is inhibited by excess bovine uterus calmodulin-binding protein (histone H2B). 6. The phosphorylation of myelin basic protein by phosphorylase kinase is partially inhibited, whereas the phosphorylation of uterus calmodulin-binding protein (histone H2B) is unaffected by calmodulin or troponin C. 7. The subcellular distribution of myelin basic protein and calmodulin suggests that the two proteins do not exist as a complex in vivo.

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

scholarly journals The Major Acid-soluble Proteins of Bacillus subtilis Spores: Partial Amino Acid Sequence and Forespore Location of Their mRNAs

Microbiology ◽  
1987 ◽  
Vol 133 (8) ◽  
pp. 2237-2246
Author(s):  
H. BLOM ◽  
R. MORSE ◽  
J. MANDELKORN ◽  
M. ARNAUD ◽  
R. WARBURG ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Soluble Proteins ◽  
Partial Amino Acid Sequence ◽  
Major Acid
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