Abstract
The interaction of troponin-I (TN-I) and troponin-T (TN-T) was examined using immobilized TN-I as an affinity adsorbent. TN-T dissolved in 0.4 M NaCl bound strongly to immobilized TN-I and required the application of 5 M urea for its elution. A chymotryptic fragment of TN-T (Ohtsuki, 1978), perhaps the C-terminal fragment, retained the ability of the original TN-T to bind to immobilized TN-I.