Cardiac High Molecular Weight Calmodulin Binding Protein Contains Calpastatin Activity†

Biochemistry ◽  
1997 ◽  
Vol 36 (39) ◽  
pp. 11550-11555 ◽  
Author(s):  
Rakesh Kakkar ◽  
Rajala V. S. Raju ◽  
Ronald L. Mellgren ◽  
Jasim Radhi ◽  
Rajendra K. Sharma
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Binding Protein ◽  
Calmodulin Binding

Cardiac high molecular weight calmodulin-binding protein is homologous to calpastatin I and calpastatin II

2008 ◽  
Vol 373 (3) ◽  
pp. 387-391 ◽  
Author(s):  
Nisha Singh ◽  
Anuraag Shrivastav ◽  
Doug Olson ◽  
Ashakumary Lakshmikuttyamma ◽  
Andrew Ross ◽  
...  
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Binding Protein ◽  
Calmodulin Binding

scholarly journals The cytoskeletal system of nucleated erythrocytes. II. presence of a high molecular weight calmodulin-binding protein.

1982 ◽  
Vol 95 (1) ◽  
pp. 278-284 ◽  
Author(s):  
D C Bartelt ◽  
R K Carlin ◽  
G A Scheele ◽  
W D Cohen
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Binding Protein ◽  
Mammalian Species ◽  
Apparent Molecular Weight ◽  
Cytoskeletal Proteins ◽  
Calcium Dependent ◽  
Calmodulin Binding ◽  
Marginal Band ◽  
Band Material

Calmodulin was detected in dogfish erythrocyte lysates by means of phosphodiesterase activation. Anucleate dogfish erythrocyte cytoskeletons bound calmodulin. Binding of calmodulin was calcium-dependent, concentration-dependent, and saturable. Cytoskeletons consisted of a marginal band of microtubules containing primarily tubulin, and trans-marginal band material containing actin and spectrinlike proteins. Dogfish erythrocyte ghosts and cytoskeletons were found to contain a calcium-dependent calmodulin-binding protein, CBP, by two independent techniques: (a) 125I-calmodulin binding to cytoskeletal proteins separated by SDS PAGE, and (b) in situ azidocalmodulin binding in whole anucleate ghosts and cytoskeletons. CBP, with an apparent molecular weight of 245,000, co-migrated with the upper band of human and dogfish erythrocyte spectrin. CBP was present in anucleate ghosts devoid of marginal bands and absent from isolated marginal bands. CBP therefore appears to be localized in the trans-marginal band material and not in the marginal band. Similarities between CBP and high molecular weight calmodulin-binding proteins from mammalian species are discussed.

Role of High Molecular Weight Calmodulin Binding Protein in Cardiac Muscle

2003 ◽  
pp. 285-302
Author(s):  
Lakshmikuttyamma Ashakumary ◽  
Rakesh Kakkar ◽  
Ponniah Selvakumar ◽  
Mohammed Khysar Pasha ◽  
Rajendra K. Sharma
Keyword(s):  
Molecular Weight ◽  
Cardiac Muscle ◽  
High Molecular Weight ◽  
Binding Protein ◽  
Calmodulin Binding
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