The optical-rotatory dispersion of myosin A

作者: Yuji Tonomura , Kazuko Sekiya , Kiichi Imamura

DOI: 10.1016/0006-3002(63)91262-9

关键词:

摘要: Effects of dioxane and p-chloromercuribenzoate (PCMB) on the optical-rotatory dispersion myosin A were measured in 0.6 M KCl at pH 7.0 compared with those ATPase activity. The α-helical content estimated from b0 term Moffitt-Yang plot was 57–61%. On addind 8–10 volume percent dioxane, increase helical by several pronounced activation firstly observed followed gradual decreases 2 h after addition decreased only a few percent, while activity disappeared completely. Immediately specific rotatory power 5000 showed its maximum about 10% accordance ATPase. alkaline-inactivated A, however, remained constant dioxane. adding PP1 before various times shift caused depressed completely during measurements. 3–4 moles PCMB per 105 g velocity Michaelis 20° increased, respectively, 0.22 to 0.44 mmoles P1/min/g 1.3 1.5·104M, temperature dependence increased significantly, 8 inhibited. 4 g. presence ATP or PP1, fell between either two. basis these other observations, it suggested that conformation active site is very susceptible influences that, accordingly, minute change induces

参考文章(49)
Manuel F. Morales, Ken Hotta, The Adenosine Triphosphatase Activity of Myosin B Treated with S-β-Aminoethylisothiuronium Journal of Biological Chemistry. ,vol. 235, pp. 1979- 1986 ,(1960) , 10.1016/S0021-9258(18)69349-4
A. Stracher, Spectrophotometric Titration and Ultraviolet Difference Spectra of Myosin and the Meromyosins Journal of Biological Chemistry. ,vol. 235, pp. 2302- 2306 ,(1960) , 10.1016/S0021-9258(18)64617-4
Junko Yoshimura, Yuji Tonomura, Shotaro Kitagawa, On the active site of myosin A-adenosine triphosphatase. II. Properties of the trinitrophenyl enzyme and the enzyme free from divalent cations Journal of Biological Chemistry. ,vol. 236, pp. 902- 906 ,(1961)
Sam Yanari, F.A. Bovey, Interpretation of the ultraviolet spectral changes of proteins. Journal of Biological Chemistry. ,vol. 235, pp. 2818- 2826 ,(1960) , 10.1016/S0021-9258(18)64546-6
J. Gergely, THE INTERACTION BETWEEN ACTOMYOSIN AND ADENOSINE TRIPHOSPHATE. LIGHT SCATTERING STUDIES Journal of Biological Chemistry. ,vol. 220, pp. 917- 926 ,(1956) , 10.1016/S0021-9258(18)65316-5
Lawrence B. Smillie, Cyril M. Kay, Abnormal Tyrosine Ionization and Configurational Changes of Trypsinogen in Alkaline Solutions Journal of Biological Chemistry. ,vol. 236, pp. 112- 117 ,(1961) , 10.1016/S0021-9258(18)64438-2
W. Wayne Kielley, Louise B. Bradley, The relationship between sulfhydryl groups and the activation of myosin adenosinetriphosphatase. Journal of Biological Chemistry. ,vol. 218, pp. 653- 659 ,(1956) , 10.1016/S0021-9258(18)65832-6
A.N. Glazer, Emil L. Smith, Phenolic hydroxyl ionization in papain. Journal of Biological Chemistry. ,vol. 236, pp. 2948- 2951 ,(1961) , 10.1016/S0021-9258(19)76407-2
Woju Ionomura, Kazuko Sekiya, Kiichi Imamura, Tomonobu Tokiwa, The optical-rotatory dispersion of myosin A Biochimica et Biophysica Acta. ,vol. 69, pp. 305- 312 ,(1963) , 10.1016/0006-3002(63)91263-0