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- W211573625 abstract "Tomato ACC synthase is inactivated by its substrate SAM, with the moiety of aminobutyrate being covalently linked to ACC synthase during the catalytic reactions. A partial purified ACC synthase (the catalytic activity 100 {mu}mol/h{center dot}mg protein) from pellets of apple extract was incubated with (3,4{sup 14}C) SAM. Only one radioactive peak was revealed in a C-4 reverse phase HPLC and one radioactive band on SDS-PAGE with an M.W. of 48 kDa. Apple ACC synthase in native form is resistant to V8, {alpha}-chromtrypsin and carboxylpeptidase A digestion, but effectively inactivated by trypsin and ficin, as demonstrated by both the activity assay and SAM labeling. The radioactive protein cut from the SDS-PAGE was injected to three mice, two of the mice showed responses to the protein in western blot analysis. The antibodies from mice is currently under characterization." @default.
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- W211573625 date "1989-04-01" @default.
- W211573625 modified "2023-09-28" @default.
- W211573625 title "Purification of 1-aminocyclopropane-1-carboxylate synthase from apple fruits using s-adenosyl (3,4 sup 14 C)-methionine (SAM) as a probe" @default.
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