By S. F. Yang (auth.), Yoram Fuchs, Edo Chalutz (eds.)
Read or Download Ethylene: Biochemical, Physiological and Applied Aspects, An International Symposium, Oiryat Anavim, Israel held January 9–12 1984 PDF
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Extra resources for Ethylene: Biochemical, Physiological and Applied Aspects, An International Symposium, Oiryat Anavim, Israel held January 9–12 1984
5 The physiological relevance of the membrane associated enzyme detected in vitro can be studied by comparing it with the conversion activity studied at the tissue level. (a) Specificity - both the membrane and the tissue activities show a marked preference for ACC as substrate. When ACC analogs are added, no ethylene is formed. Moreover, the presence of analogs does not inhibit the ACC conversion activity in either system (Table 4). (b) Inhibitors - both the enzyme and the tissue activities are inhibited by free radical scavengers such as Tiron (8), and propyl gallate (4), indicating that free radicals are required for the reaction to proceed.
4) (8). Continued focusing under --.. 12 0 0 . - - - -- - - -- -- - - , 1000 S _ pH 0--- Prot .... tane. (em) FIGURE 3. PAGE pattern for Triton X-IOO extract of mung bean ext racts. FIGURE 4. Isoelectric focusing pattern of Triton X-IOO extract from mung bean sprouts. pH 6-8 ampholite. these conditions did not change the position of the band with respect to pH. 5. If focusing was continued for many hours at 1500 volts, the binding component was lost. One of the problems with isoelectric focusing is that the gradient will drift toward the anode 52 end after prolonged periods at high voltages, thus limiting the usefulness of the technique.
G. lipid peroxides) may be involved. This contention is supported by the finding that the conversion of ACC to ethylene by these membranes is stimulated by lipoxygenase and linolenic acid (Fig. 2F), an exogenous source of lipid hydroperoxides, and inhibited in the presence of glutathione peroxidase and glutathione (Fig. 2G), which catalyse the reduction of hydroperoxides (12). The conversion of ACC to ethylene by pea microsomal membranes is also inhibited by 1 roM n-propyl gallate (Fig. 2H), an observation that implicates the involvement of free radicals, and evidence obtained by electron spin resonance (ESR) spectroscopy indicates that the superoxide anion (02T) is required for ethylene production in this system.