Purification and Synthesis under Anaerobic Conditions of Rice Arginine Decarboxylase |
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Authors: | Reggiani Remo |
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Institution: | Istituto Biosintesi Vegetali, C.N.R. via Bassini 15, 1-20133, Milano, Italy |
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Abstract: | Arginine decarboxylase (ADC; EC 4.1.1.19
EC]
) which catalyzes thesynthesis of putrescine, is involved in the responses of plantsto stress. The enzyme was purified 1,561-fold from rice coleoptilesby steps that included ammonium sulfate fractionation, gel filtration,ion-exchange chromatography and chromatofocusing. The purifiedenzyme had a pI of 5.3, a molecular mass of 176 kDa and appearedto be composed of three subunits of 63 kDa. A polyclonal antibodywas raised in a rabbit and the IgG fraction was purified fromserum. On Western blots the antibody recognized the ADC fromboth rice and E. coli. Immunoprecipitation with the ADC-specificantibodies allowed detection of radiolabelled ADC in extractsfrom aerobically and anaerobically grown rice seedlings thathad been supplied with a mixture of 14C-amino acids. This resultis discussed in relation to the role of ADC under anaerobicconditions. (Received April 28, 1994; Accepted September 27, 1994) |
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