Protochlorophyll(IDE) holochrome subunits from a mutant defective in the regulation of protochlorophyll(IDE) synthesis

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Purification of protochlorophyllide holochrome.

Phototransformable protochlorophyllide holochrome was prepared from etiolated bean leaves. The detergent Triton X-100 in the presence of glycerol and tricine-KOH buffer (pH 8) enhanced the extractability, specific activity, and phototransformability of the holochrome. Purification was achieved by polyethylene glycol-6000 precipitation and hydroxyl-apatite, DEAE-cellulose, and agarose chromatogr...

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Enzymic nature of the protein moiety of protochlorophyllide holochrome.

The enzymic nature of the protein moiety of protochlorophyll(ide) holochrome was studied by following the fate of the [(14)C]protochlorophyll(ide) formed when dark-grown barley (Hordeum vulgare) or bean (Phaseolus vulgaris) leaves are incubated in the dark with 3 mm 4-delta-[(14)C]aminolevulinic acid. It was found that: [List: see text]Since turnover of protochlorophyll(ide) was not observed, t...

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Energy Transfer from NADPH to Protochlorophyllide in Isolated Protochlorophyllide Holochrome as Determined by UV-Fluorescence Excitation Spectroscopy at 77 K

The low -tem perature fluorescence excitation analysis o f different pro tochlorophyllide (PChlide) form s has been extended to the UV part o f the spectrum . A new band at abou t 360 nm was detected in excitation spectra o f active PChlide forms bound to isolated p ro to ­ chlorophyllide holochrom e. This band is very similar to the absorbance o f N A D P H in this region and its intensity dep...

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Immunological distinction between fraction I protein and protochlorophyllide holochrome.

Ribulose 1,5-diphosphate carboxylase (RuDP carboxylase) has been shown to be the major component of the Fraction I protein of leaves (5, 6). Protochlorophyllide associated with a protein, i.e. protochlorophyllide holochrome (PCH), has been isolated from etiolated bean leaves (1, 9,10); upon illumination in zirvo or in vitro it is transformed into chlorophyllide holochrome. Several investigators...

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Analysis of the subunit structure of protochlorophyllide holochrome by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

The subunit structures of protochlorophyllide holochrome (PCH) and chlorophyllide holochrome (CH) were studied by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. PCH from leaves of dark-grown (Phaseolus vulgaris var. red kidney) is a polymeric pigment-protein complex of approximately 600,000 daltons. It is composed of 12 to 14 polypeptides of 45,000 daltons, when examined prior...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 1973

ISSN: 0014-5793

DOI: 10.1016/0014-5793(73)80517-4