scholarly journals Calcium-binding modulator protein from the unfertilized egg of the sea urchin Arbacia punctulata.

1979 ◽  
Vol 80 (1) ◽  
pp. 211-218 ◽  
Author(s):  
J F Head ◽  
S Mader ◽  
B Kaminer
Keyword(s):  
Sea Urchin ◽  
Calcium Binding ◽  
Troponin I ◽  
Binding Protein ◽  
Bovine Brain ◽  
Calcium Binding Protein ◽  
Free Calcium ◽  
Affinity Column ◽  
Arbacia Punctulata ◽  
Peptide Map

We have purified and partly characterized a calcium-binding protein from the unfertilized egg of the sea urchin Arbacia punctulata. This protein closely resembles the calcium-binding modulator protein of bovine brain in its molecular weight, electrophoretic mobility, amino acid analysis, and peptide map. It activates bovine brain phosphodiesterase in the presence of calcium but has no effect on the phosphodiesterase of the Arbacia egg. Densitometric scanning of acrylamide gels of arbacia egg homogenates shows the modulator protein to represent 0.1% of the total protein of the egg. At 10(-4) M free calcium, the protein binds four calcium ions per 17,000-dalton molecule. We have used a column of rabbit skeletal muscle troponin-I covalently coupled to Sepharose 4B as an affinity column to selectively purify the Arbacia egg calcium-binding protein. This column has also been used to purify bovine brain modulator protein and may prove of general use in isolating similar proteins from other sources. The technique may be particularly helpful when only small quantities of starting material are available.

scholarly journals Identification of a novel calcium binding protein from bovine brain

FEBS Letters ◽  
1983 ◽  
Vol 164 (1) ◽  
pp. 80-84 ◽  
Author(s):  
David Morton Waisman ◽  
Judith Muranyi ◽  
Ahmed Mohammed
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Bovine Brain ◽  
Calcium Binding Protein

scholarly journals The amino acid sequence, immunofluorescence and microinjection studies on the 15kDa calcium-binding protein from sea urchin egg.

1988 ◽  
Vol 13 (6) ◽  
pp. 525-532 ◽  
Author(s):  
Hiroshi Hosoya ◽  
Takashi Takagi ◽  
Issei Mabuchi ◽  
Hisashi Iwaasa ◽  
Hikoichi Saka ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sea Urchin ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Sea Urchin Egg

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.

scholarly journals Neurocalcin: a novel calcium-binding protein from bovine brain.

1992 ◽  
Vol 267 (27) ◽  
pp. 19596-19599 ◽  
Author(s):  
M Terasawa ◽  
A Nakano ◽  
R Kobayashi ◽  
H Hidaka
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Bovine Brain ◽  
Calcium Binding Protein

Isolation of a calreticulin-like calcium binding protein from bovine brain

1992 ◽  
Vol 12 (1-3) ◽  
pp. 69-76 ◽  
Author(s):  
Robin J. Johnson ◽  
Ningai Liu ◽  
Jordan B. Fishman ◽  
J.D. Dixon ◽  
Richard E. Fine
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Bovine Brain ◽  
Calcium Binding Protein
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