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A comparative study of the cardiac troponin inhibitory factor (TNI) from mammalians


A comparative study of the cardiac troponin inhibitory factor (TNI) from mammalians



Pflugers Archiv: European Journal of Physiology 374(3): 277-283



ISSN/ISBN: 0031-6768

PMID: 209399

DOI: 10.1007/bf00585605

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.

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Accession: 039047169

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