scholarly journals Phosphorylation of the ‘37000 component’ of the troponin complex (troponin-T)

1973 ◽  
Vol 131 (2) ◽  
pp. 425-428 ◽  
Author(s):  
S. V. Perry ◽  
H. A. Cole
Keyword(s):  
Calcium Binding ◽  
Troponin T ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Inhibitory Protein ◽  
Troponin Complex

Most of the phosphorus present in the troponin complex, which on average contains 1 mol of P/80000g, is associated with the ‘37000 component’ (0.6mol of P/mol). The inhibitory protein and particularly the ‘37000 component’, but not the calcium-binding protein, were phosphorylated when incubated with phosphorylase b kinase and [γ-32P]ATP.

scholarly journals The interaction of the calcium-binding protein (troponin C) with bivalent cations and the inhibitory protein (troponin I)

1974 ◽  
Vol 137 (2) ◽  
pp. 145-154 ◽  
Author(s):  
J. F. Head ◽  
S. V. Perry
Keyword(s):  
Skeletal Muscle ◽  
Calcium Binding ◽  
Troponin I ◽  
Binding Protein ◽  
Sodium Dodecyl ◽  
Psoas Muscle ◽  
Calcium Binding Protein ◽  
Sedimentation Equilibrium ◽  
Free Form ◽  
Inhibitory Protein

1. The molecular weight of the calcium-binding protein of rabbit white skeletal muscle was estimated to be 18500 by sedimentation equilibrium and electrophoresis in sodium dodecyl sulphate. 2. Addition of 2 Ca2+ ions per molecule produced reversible changes in the u.v.-absorption spectrum that are interpreted as arising from conformational changes in the structure of the protein. 3. Cd2+ was almost as effective as Ca2+ in producing the spectral changes. Other bivalent metal ions, particularly Mg2+, were less effective. 4. Binding of Ca2+ by the calcium-binding protein produced an increase in mobility to the anode on electrophoresis in 6m-urea at pH8.6. The Ca2+-saturated form of the protein was more retarded on gel filtration than the Ca2+-free form. 5. In the presence of Ca2+ the calcium-binding protein formed an equimolar complex with the inhibitory protein. This complex was stable in 8m-urea and in the pH range 7.0–8.6. 6. An isotope-dilution method for the measurement of the content of calcium-binding protein in whole muscle is described. In rabbit psoas muscle the ratio of actin monomers to molecules of calcium-binding protein was approx. 7:1. Similar values were obtained for red skeletal and cardiac muscle. 7. Evidence is presented indicating that in the rabbit the inhibitory protein of the troponin complex of red skeletal and cardiac muscles is different from the inhibitory protein of white skeletal muscle.

Calcium-binding protein 1 of Entamoeba histolytica transiently associates with phagocytic cups in a calcium-independent manner

2008 ◽  
Vol 10 (6) ◽  
pp. 1373-1389 ◽  
Author(s):  
Ruchi Jain ◽  
Julien Santi-Rocca ◽  
Narendra Padhan ◽  
Sudha Bhattacharya ◽  
Nancy Guillen ◽  
...  
Keyword(s):  
Entamoeba Histolytica ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Independent Manner ◽  
Phagocytic Cups

scholarly journals Regulation of adenylate cyclase from glial tumor cells by calcium and a calcium-binding protein.

1976 ◽  
Vol 251 (15) ◽  
pp. 4744-4750 ◽  
Author(s):  
M A Brostrom ◽  
C O Brostrom ◽  
B M Breckenridge ◽  
D J Wolff
Keyword(s):  
Adenylate Cyclase ◽  
Tumor Cells ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Glial Tumor
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