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A new method for isolating physiologically active Mg-protoporphyrin monomethyl ester, the substrate of the cyclase enzyme of the chlorophyll biosynthetic pathway.

A new method for isolating physiologically active Mg-protoporphyrin monomethyl ester, the substrate of the cyclase enzyme of the chlorophyll biosynthetic pathway. Research Abstract Details 

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  • A new method for isolating physiologically active Mg-protoporphyrin monomethyl ester, the substrate of the cyclase enzyme of the chlorophyll biosynthetic pathway. Abstract Text:

    simon p goughSimon P Gough,kamila rzeznickaKamila Rzeznicka,ragna peterson wulffRagna Peterson Wulff,jose da cruz franciscoJose da Cruz Francisco,andreas hanssonAndreas Hansson,poul erik jensenPoul Erik Jensen,mats hanssonMats Hansson,simon p goughSimon P Gough,kamila rzeznickaKamila Rzeznicka,ragna peterson wulffRagna Peterson Wulff,jose da cruz franciscoJose da Cruz Francisco,andreas hanssonAndreas Hansson,poul erik jensenPoul Erik Jensen,mats hanssonMats Hansson,

    Mg-protoporphyrin monomethyl ester (MPE) is a biosynthetic intermediate of chlorophyll and converted by MPE cyclase to protochlorophyllide. Limited availability of MPE has so far hampered cyclase research. In a new, simplified, method MPE was prepared from freeze dried bchE mutant Rhodobacter capsulatus DB575 cells by extraction with acetone/H(2)O/25% NH(3). Isolated MPE was identified by absorption and fluorescence spectroscopy, and its purity was analyzed by HPLC. The extracted MPE was dried and redissolved in buffered DMSO and its substrate activity is shown by enzymatic cyclase assays. A linear time course was observed for MPE conversion to protochlorophyllide by enzymes from barley etioplasts. Our innovation of freeze drying the R. capsulatus cells before extraction provides a high yield method for MPE, which is significantly faster and more reproducible than previous extraction methods.

    A new method for isolating physiologically active Mg-protoporphyrin monomethyl ester, the substrate of the cyclase enzyme of the chlorophyll biosynthetic pathway. Publishing Authors By Initials

    sp goughSP Gough,k rzeznickaK Rzeznicka,r peterson wulffR Peterson Wulff,jda franciscoJda Francisco,a hanssonA Hansson,pe jensenPE Jensen,m hanssonM Hansson,sp goughSP Gough,k rzeznickaK Rzeznicka,r peterson wulffR Peterson Wulff,jda franciscoJda Francisco,a hanssonA Hansson,pe jensenPE Jensen,m hanssonM Hansson,

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    A new method for isolating physiologically active Mg-protoporphyrin monomethyl ester, the substrate of the cyclase enzyme of the chlorophyll biosynthetic pathway. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Plant physiology and biochemistry : PPB / Société

    VOLUME: 45

    Page Numbers: 932-6

    Journal Abbreviation: Plant Physiol. Biochem.

    ISSN: 0981-9428

    DAY: 14

    MONTH: 09

    YEAR: 2007

    A new method for isolating physiologically active Mg-protoporphyrin monomethyl ester, the substrate of the cyclase enzyme of the chlorophyll biosynthetic pathway. Information

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    LANGUAGE: eng

    NlmUniqueID: 9882449

    A new method for isolating physiologically active Mg-protoporphyrin monomethyl ester, the substrate of the cyclase enzyme of the chlorophyll biosynthetic pathway. Keywords Mesh Terms:

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    Grant and Affiliation Information for A new method for isolating physiologically active Mg-protoporphyrin monomethyl ester, the substrate of the cyclase enzyme of the chlorophyll biosynthetic pathway.

    AFFILIATION: Department of Biochemistry, Lund University, Box 124, SE-22100 Lund, Sweden.

    Country: France

    France Research PublicationFrance Research Publication

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    MEDLINETA: Plant Physiol Biochem

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