propyl gallate/glycine max

The ability of 19 structural analogs of propyl gallate to inhibit purified soybean seed (Glycine max [L.] Merr. var. Ransom) lipoxygenase-2 (EC 1.13.11.12) was determined. The results indicate that the o-dihydroxy and not the ester function of propyl gallate is essential for inhibition of

Three lipoxygenase isozymes are synthesized in developing soybean (Glycine max [L.] Merr. cv Williams) embryos and are found in high levels in cotyledons of mature seeds (B Axelrod, TM Cheesbrough, S Zimmer [1981] Methods Enzymol 71: 441-451). Upon germination at least two new protein species appear

A disengagement of the cyanide-resistant, alternative respiratory pathway in soybean (Glycine max (L.) Merr.) callus tissue was observed prior to the start of deoxyisoflavone production stimulated by addition of the cytokinin benzyladenine. To test whether this loss of alternativepathway activity

Mitochondria from axes of Glycine max (L.) Merr. cv. Chippewa 64 seedlings purified on discontinuous Percoll gradients exhibited classical cyanide-resistant respiration. These mitochondria also possessed lipoxygenase activity, as determined by O(2) uptake in the presence of 0.8 millimolar linoleic

The initial burst of respiratory activity (Q(o) (2)) of imbibing soybean (Glycine max [L.] Merr. var. Wayne) seed tissue is cyanide-insensitive, and sensitive to salicylhydroxamate: presumptive evidence for the presence of alternate respiration. The initial O(2) consumption is also highly sensitive

Highly purified soybean (Glycine max L. Merr.) plasma membranes exhibit a lipoxygenase activity with a pH optimum in the acidic (5.5-6.0) range and with a Km value of 200 microM for both linolenic and linoleic acids. This activity is inhibited by nordihydroguaiaretic acid (NDGA), salicylhydroxamic