Cross-linking of troponin with dimethylimido esters

Abstract

The topology of troponin, the calcium binding regulatory protein in muscle, has been studied by cross-linking with different length dimethylimido esters. The results show that the three components of troponin are close to each other and that the troponin-I and -T are preferentially cross-linked being 0.6 nm or less apart. The largest cross-linked product is a complex which corresponds in molecular weight to the native troponin complex of 1 mol of each of the three components. Cross-linked troponin has lost the ability to make the actomyosin ATPase calcium sensitive although it does bind to actin-tropomyosin and tropomyosin, and it binds calcium normally. No effect of calcium on cross-linking could be detected.