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• W2034382851 abstract "Abstract 1. 1. 1 mole of 1-dimethylaminonaphthalene-5-sulfonyl chloride (DNS) reacted selectively with 1 mole of lysine residue per 3.6·10 5 g (approx.) of heavy meromyosin quantitatively to form a sulfonamide linkage, and the labeling of heavy meromyosin with DNS was interrupted by addition of ATP to the incubation medium. 2. 2. By labeling with 1 mole of DNS per 1 mole of heavy meromyosin, heavy meromyosin ATPase (ATP phosphohydrolase, EC 3.6.1.3) activity was completely inhibited either in the presence of 5 mM CaCl 2 or 0.5 M KCl. However, when the ATPase activity was measured under the conditions where both 5 mM CaCl 2 and 0.5 M KCl were present in the reaction mixture, the ATPase activity of heavy meromyosin, which was labeled to the extent of 1 mole of DNS per 1 mole of heavy meromyosin, was about 80% of the control value (the activity of non-labeled heavy meromyosin ATPase). Labeling with DNS caused a decrease in K m and v max of heavy meromyosin ATPase and a marked increase in the Arrhenius activation energy over the higher temperature range (above 13°). Addition of 1-dimethylaminonaphthalene-5-sulfonic acid (DNS-OH) to the reaction mixture caused a decrease in K m and v max of heavy meromyosin ATPase as well as in extent of DNS labeling. DNS-labeled heavy meromyosin ATPase showed no depression of the activity around neutral pH and was not activated by p -chloromercuribenzoate (PCMB), in contrast with non-labeled enzyme. Furthermore, it was not activated by F-actin at low ionic strength in the presence of Mg 2− . 3. 3. K m and v max of DNS-labeled heavy meromyosin ATPase were markedly decreased by addition of urea, ethanol, dioxane or propylene glycol, compared with those of non-labeled one. However, decreases in the helical content of DNS-labeled heavy meromyosin induced by denaturants were almost the same as those in the helical content of non-labeled heavy meromyosin ATPase. 4. 4. 3.5 moles of −SH groups per 1·10 5 g protein were masked by labeling with 0.28 mole of DNS per 1·10 5 g protein (equivalent to 1 mole of DNS per 1 mole of heavy meromyosin). Based on these results, the chemical and physicochemical properties of the active site of heavy meromyosin ATPase are discussed." @default.
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• W2034382851 date "1970-02-01" @default.
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• W2034382851 title "Fluorescent probe for active site of heavy meromyosin I. Changes in enzymic properties by labeling with i-dimethylaminonaphthalene-5-sulfonyl chloride" @default.
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• W2034382851 doi "https://doi.org/10.1016/0005-2795(70)90174-1" @default.
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