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The histochemical distribution of protein bound sulfhydryl groups in human epidermis by the new staining method.
A new fluorescent thiol reagent, N-(7-dimethylamino-4-methylcoumarinyl)-maleimide (DACM) which is nonfluorescent by itself but will react readily with -SH groups to form highly fluorescent addition products is synthesized and studied the localization and concentration of -SHgroups and S--S linkages in the human epidermis. Expand
A streamlined method of subfragment one preparation from myosin.
A rapid procedure for isolating subfragment one (SF1) from myosin was found and how important quick preparation of SF1 is for maintaining the active site structure was indicated. Expand
An immunoglobulin G inhibiting lactate dehydrogenase activity.
The anti-LDH activity gradually decreased with a half-life of 20 days corresponding to that of IgG and finally almost disappeared, indicating a possibility that the myoma cells produce some factors such as B-cell growth and differentiation factors. Expand
A new, smaller actin-activatable myosin subfragment 1 which lacks the 20-kDa, SH1 and SH2 peptide.
The results show that SH1 and SH2 are not essential for ATPase activity and that binding of actin to the 20-kDa region is notessential for the enhancement of the Mg2+-ATPase activity. Expand
Thiols of myosin. IV. "Abnormal" reactivity of S1 thiol and the conformational changes around S2 thiol.
Kinetic analysis showed that the teritiary structure around S1 at alkaline pH differed from that at acidic pH, and non-linearity of the Arrhenius plots of the reaction rate of S2 suggested that the S2 region of myosin had different conformations at high and low temperatures, the transition temperature being 10--15degrees. Expand
Actin-induced local conformational change in the myosin molecule. III. Reactivity of S2 thiol and DTNB-reactive thiols of porcine cardiac myosin.
The third or most slowly reacting thiol group, was found to be remarkably susceptible to Ca2+ at physiological concentrations (10(-8)-10(-6) M) in the presence of Mg2+-ADP for cardiac myosin, but in striking contrast, in the absence of a relatively long-lived intermediate of myOSin ATPase, the structure of which may be different in cardiac and skeletal myosins. Expand
The enzymic properties of N-ethylmaleimide modified myosin
Abstract The catalytic properties of native myosin and of myosin in which one SH-group per subunit chain has been blocked with N-ethylmaleimide have been compared. The Ca2+-ATPase activity of thisExpand
Fluorescent thiol reagents. VI. N-(1-Anilinonaphthyl-4)maleimide; a fluorescent hydrophobic probe directed to thiol groups in protein.
In the fluorescence spectra of the reaction products of ANM with thiols, the quantum yields increase and the emission maxima shift towards the blue as the solvent polarity decreases, and ANM is thus expected to be a useful fluorescent hydrophobic probe directed to thiol groups in protein. Expand