Separation and characterization of the 37 000 dalton component of the troponin system

Reexamination of the conformation of muscle proteins by optical activity

“…I agree with those reported by Oikawa et al (1968) and Staprans and Watanabe (1970). Our CD extrema of TN-C and TN-T are higher than those reported by Kay and co-workers but those for TN-I are slightly lower (Murray and Kay, 1972;Maní et al, 1973Maní et al, , 1974b. Our CD extrema for the light chains of myosin are comparable to those of Lowey and Holt (1972).…”

“…In our case, the maximum impurity amounts to about 5% for myosin, which is as purified as can be achieved at present. Another possible source of error is the determination of protein concentrations by various methods such as ultraviolet absorptivity (Nagy and Strzelecka-Golaszewska, 1972;Murphy, 1974;Maní et al, 1974b), colorimetry (Murphy, 1971(Murphy, , 1974Maní et al, 1973), and synthetic boundary by analytical ultracentrifuge (Murray and Kay, 1972). For instance, TN-C was reported to have an £277.5 °f 2.3 (Murray and Kay, 1972) or £^0 of 1.4 (van Eerd and Kawasaki, 1973); £280 for TN-I ranges from 2.9 (van Eerd and Kawasaki, 1973), to 3.97 (Wilkinson, 1974), to 6.6 (Maní et al, 1974a), and that for TN-T is 4.4, 5.0, and 3.7 by the same workers (although Wilkinson and Maní et al used the same Rayleigh fringe numbers per unit concentration).…”