Physicochemical studies on the interaction of the calcium-binding protein (troponin C) with the inhibitory protein (troponin I) and calcium ions

Biochemistry ◽  
1974 ◽  
Vol 13 (13) ◽  
pp. 2689-2694 ◽  
Author(s):  
William D. McCubbin ◽  
R. S. Mani ◽  
Cyril M. Kay
Keyword(s):  
Calcium Ions ◽  
Calcium Binding ◽  
Troponin I ◽  
Binding Protein ◽  
Troponin C ◽  
Calcium Binding Protein ◽  
Inhibitory Protein ◽  
Physicochemical Studies

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.

The amino acid sequence of porcine intestinal calcium-binding protein

1979 ◽  
Vol 57 (6) ◽  
pp. 737-748 ◽  
Author(s):  
Theo Hofmann ◽  
Michiko Kawakami ◽  
Anthony J. W. Hitchman ◽  
Joan E. Harrison ◽  
Keith J. Dorrington
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Intestinal Mucosa ◽  
Calcium Binding ◽  
Binding Protein ◽  
Troponin C ◽  
Calcium Binding Protein ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

The complete amino acid sequence of the calcium-binding protein (CaBP) from pig intestinal mucosa has been determined: Ac-Ser-Ala-Gln-Lys-Ser-Pro-Ala-Glu-Leu-Lys-Ser-Ile-Phe-Glu-Lys-Tyr-Ala-Ala-Lys-Glu-Gly-Asp-Pro-Asn-Gln-Leu-Ser-Lys-Glu-Glu-Leu-Lys-Gln-Leu-Ile-Gln-Ala-Glu-Phe-Pro-Ser-Leu-Leu-Lys-Gly-Pro-Arg-Thr-Leu-Asp-Asp-Leu-Phe-Gln-Glu-Leu-Asp-Lys-Asn-Gly-Asn-Gly-Glu-Val-Ser-Phe-Glu-Glu-Phe-Gln-Val-Leu-Val-Lys-Lys-Ile-Ser-Gln-OH. The N-terminal octapeptide sequence was determined by mass spectrometry analysis by Morris and Dell. The first 45 residues of bovine CaBP differ only in six positions from the corresponding sequence of the porcine protein, except that the sequence starts in position two of the porcine sequence. The mammalian intestinal CaBP's belong to the troponin-C superfamily on the basis of an analysis by Barker and Dayhoff.

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 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.

Analysis of the complete sequence of a muscle calcium-binding protein of Schistosoma mansoni

Parasitology ◽  
1992 ◽  
Vol 105 (3) ◽  
pp. 399-408 ◽  
Author(s):  
T. J. Stewart ◽  
A. L. Smith ◽  
J. C. Havercroft
Keyword(s):  
Schistosoma Mansoni ◽  
Light Chain ◽  
Calcium Binding ◽  
Binding Protein ◽  
Complete Sequence ◽  
Regulatory Light Chain ◽  
Troponin C ◽  
Calcium Binding Protein ◽  
Predicted Amino Acid Sequence ◽  
Ef Hand

SUMMARYThe complete sequence of the cDNA encoding a 20 kDa calcium-binding protein of Schistosoma mansoni (Sm20) has been determined. The predicted amino acid sequence contains 4 EF hand domains but examination of the predicted secondary structure of Sm20, together with the specific residues in each calcium-binding domain, suggests that only 1 EF hand (domain IV) is functional. Sm20 is most homologous to calmodulin, troponin C and the regulatory light-chain of myosin, particularly those of invertebrates. However, troponin C and the regulatory light-chain of myosin can be distinguished from Sm20 by size and by their differential levels of expression during the life-cycle. Sm20 also appears to be distinct from calmodulin but may be functionally equivalent to the soluble sarcoplasmic calcium-binding proteins of molluscs and crustacea which may act as a reservoir for calcium in muscle. Sm20 is encoded by a small multi-gene family whose members are clustered within a 15 kb region of the genome. A 20 kDa antigen, cross-reactive with Sm20, is expressed in Schistosoma haematobium, Fasciola hepatica and Paragonomus mexicanus.

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