Document Detail

A comparative study of the cardiac troponin inhibitory factor (TNI) from mammalians.
MedLine Citation:
PMID:  209399     Owner:  NLM     Status:  MEDLINE    
Troponin inhibitory factor, TNI, was prepared by affinity chromatography from different mammalian hearts. (i) Structure. These different TNI have the same M.W. (28000), which is higher than that found in rabbit skeletal muscle (23000). Nevertheless they differ with respect of their charge as shown by alkaline urea polyacrylamide gel electrophoresis using cardiac TNI which has previously been bound to an excess of skeletal troponin Ca2+-binding factor. These changes do not correlate with the PO4 content of TNI. They are associated with structural differences demonstrated by peptide mapping of the unfolded molecule after papain treatment. The structure of cardiac TNI from rat and rabbit differs clearly from that of crow and pig. (ii) Biological activity. These different TNI have the same inhibitory effect on skeletal actomyosin. ATPase, the same content of PO4 and the same ability to be phosphorylated in-vitro by a bovine heart c-AMP-dependent protein kinase.
G Berson; J L Samuel; B Swynghedauw
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Pflügers Archiv : European journal of physiology     Volume:  374     ISSN:  0031-6768     ISO Abbreviation:  Pflugers Arch.     Publication Date:  1978 May 
Date Detail:
Created Date:  1978-09-30     Completed Date:  1978-09-30     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0154720     Medline TA:  Pflugers Arch     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  277-83     Citation Subset:  IM    
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MeSH Terms
Adenosine Triphosphatases / antagonists & inhibitors
Chemical Phenomena
Chromatography, Affinity
Cyclic AMP / pharmacology
Electrophoresis, Polyacrylamide Gel
Muscle Proteins* / isolation & purification
Myocardium / analysis*
Protein Kinases
Troponin* / isolation & purification
Reg. No./Substance:
0/Muscle Proteins; 0/Phosphates; 0/Troponin; 60-92-4/Cyclic AMP; EC 2.7.-/Protein Kinases; EC; EC 3.6.1.-/Adenosine Triphosphatases

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