scholarly journals Isolation and characterization of a low molecular weight, calcium-binding protein from porcine cardiac muscle

1990 ◽  
Vol 52 ◽  
pp. 176
Author(s):  
Toshiya Sasaki ◽  
Hideaki Kise ◽  
Michiko Naka ◽  
Toshio Tanaka
Keyword(s):  
Molecular Weight ◽  
Cardiac Muscle ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Low Molecular Weight ◽  
Isolation And Characterization

The Isolation and Characterization of the ATPase Inhibitory Protein (TN-I) from Bovine Cardiac Muscle

1975 ◽  
Vol 53 (11) ◽  
pp. 1207-1213 ◽  
Author(s):  
L. D. Burtnick ◽  
W. D. McCubbin ◽  
C. M. Kay
Keyword(s):  
Molecular Weight ◽  
Cardiac Muscle ◽  
Calcium Binding ◽  
Sodium Dodecyl ◽  
Basic Amino Acid ◽  
Sedimentation Equilibrium ◽  
Amino Acid Residues ◽  
Inhibitory Protein ◽  
Isolation And Characterization

The inhibitory component of the troponin complex (TN-I) was purified from bovine cardiac muscle, using a combination of ion exchange and molecular exclusion chromatographies in the presence of urea. It has the ability to inhibit the Mg2+-activated ATPase (EC 3.6.1.3) of a synthetic cardiac actomyosin preparation and this inhibition is reversed by the addition of cardiac calcium binding component of troponin (TN-C). Conventional sedimentation equilibrium experiments suggest a molecular weight for cardiac TN-I of 22 900 ± 500. However, sodium dodecyl sulfate (SDS) gels indicate a molecular weight of 27 000 ± 1000. The mobility of TN-I on SDS gels may be anomalous due to the high proportion of basic amino acid residues in the protein. Cardiac TN-I and TN-C interact to form a tight complex, even in the presence of 6 M urea. The results of this study invite direct comparison with results published for rabbit skeletal TN-I.

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