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FASEB Journal
Ignatove, A., St. Louis Univ. Tech. Med., St. Louis, ME, United States
Nigos, I.G., Volcani Center, Bet Dagan, Israel
Janisn, O.S., College Dharm, Terris State Univ., Big Rapids, MI, United States
Burg, R., Volcani Center, Bet Dagan, Israel
Grueger, R.J., Volcani Center, Bet Dagan, Israel
Coscia, G.J., St. Louis Univ. Tech. Med., St. Louis, ME, United States
Jrounal initial purification of DHBO frtn SuWiumaria cuTmden,sis plant cell cullures, we reported that our most purified preparalions contained a major band al 77 kDa and minor, lower Mr bands. Here we present evidence on highly Durified Oxidase fractions from elicited S. canadensi,s cultures to indicate that DttBO is l he 77 kDa protein and lhat lower Mr bands represent an isozyme(s) of the PPO family thai copurities with it. An antibody (Ab) raised against the 77 kl)a protein and a tomato anti-PPO Ab that stains a 70 kDa band were used to monilor chromaiographic fractions by immunoblot analysis of the oxidases. Oxidase-containing eluates from DEAE-Sephadex. CM and ][iTrap Blue were compared to corresponding [tow through volumes. Bands at 77 and 87 kDa were detected with anti-DHBO Ab in eluates displaying high DHBO activity bul no in llow through fractions. PPO specific activity and immunoreactivity partilioned both in flow through and eluate fractions of the CM and ttiTrap Columm,. Estimalion of the DHBO and PPO specific activities for each step showed increasing enrichment of 1)ttBO accompanied by rising DIIBO/PPO activity ratios. Taken together these observations suggest that the two enzymes are, diffelent entities.
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Immunoblot analyses of the elicited plant enzyme, dihydrobenzophenanthridine oxidase (dhbo); evidence for resolution from a polyphenol oxidase (PPO) isozyme
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Ignatove, A., St. Louis Univ. Tech. Med., St. Louis, ME, United States
Nigos, I.G., Volcani Center, Bet Dagan, Israel
Janisn, O.S., College Dharm, Terris State Univ., Big Rapids, MI, United States
Burg, R., Volcani Center, Bet Dagan, Israel
Grueger, R.J., Volcani Center, Bet Dagan, Israel
Coscia, G.J., St. Louis Univ. Tech. Med., St. Louis, ME, United States
Immunoblot analyses of the elicited plant enzyme, dihydrobenzophenanthridine oxidase (dhbo); evidence for resolution from a polyphenol oxidase (PPO) isozyme
Jrounal initial purification of DHBO frtn SuWiumaria cuTmden,sis plant cell cullures, we reported that our most purified preparalions contained a major band al 77 kDa and minor, lower Mr bands. Here we present evidence on highly Durified Oxidase fractions from elicited S. canadensi,s cultures to indicate that DttBO is l he 77 kDa protein and lhat lower Mr bands represent an isozyme(s) of the PPO family thai copurities with it. An antibody (Ab) raised against the 77 kl)a protein and a tomato anti-PPO Ab that stains a 70 kDa band were used to monilor chromaiographic fractions by immunoblot analysis of the oxidases. Oxidase-containing eluates from DEAE-Sephadex. CM and ][iTrap Blue were compared to corresponding [tow through volumes. Bands at 77 and 87 kDa were detected with anti-DHBO Ab in eluates displaying high DHBO activity bul no in llow through fractions. PPO specific activity and immunoreactivity partilioned both in flow through and eluate fractions of the CM and ttiTrap Columm,. Estimalion of the DHBO and PPO specific activities for each step showed increasing enrichment of 1)ttBO accompanied by rising DIIBO/PPO activity ratios. Taken together these observations suggest that the two enzymes are, diffelent entities.
Scientific Publication
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