Protein Bodies from the Endosperm of Castor Bean

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Protein Bodies from the Endosperm of Castor Bean: Subfractionation, Protein Components, Lectins, and Changes during Germination.

Protein bodies from the storage endosperm of dry castor bean (Ricinus communis L.) were isolated by successive nonaqueous linear density gradient centrifugation. The isolated protein bodies were lysed by the addition of water, and the various structural components of the organelles were separated by sucrose gradient centrifugation. The matrix protein remained at the top of the gradient while th...

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Hydrolases in vacuoles from castor bean endosperm.

Vacuoles were prepared from endosperm tissue of 4-day-old castor bean seedlings (Ricinus communis var. Hale) and purified on a stepped sucrose gradient. It was shown by assays of marker enzymes that there was only trace contamination of the final preparation by other organelles (mitochondria, glyoxysomes, nuclei, spherosomes, and plastids) and by cytoplasmic components. Hydrolytic enzymes (acid...

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Quinolinic Acid Phosphoribosyltransferase from Castor Bean Endosperm

Quinolinic acid phosphoribosyltransf erase was purified WI-fold from the endosperm of etiolated seedlings of Ricinus communis L. Sodium dodecyl sulfate disc gel electrophoresis indicated that the enzyme was homogeneous but on analytical disc gel electrophoresis at pH 7.0 and 8.3 the isolated native protein exhibited three closely migrating bands. The three proteins were of the same molecular we...

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Proteases and Peptidases of Castor Bean Endosperm

The endosperm of castor bean seeds (Rkinus comunuis L.) contains two -SH-dependent amptidases, one hydrolyzing L-leucine-,Bnaphthylamide optimally at pH 7.0, and the other hydrolyzing L-proline,B-naphthylamide optimally at pH 7.5. After germination the endosprm contains in addition an -SH-dependent hemoglobin protease, a serinedependent carboxypeptidase, and at least two -SH-dependent enzymes h...

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Albumin storage proteins in the protein bodies of castor bean.

Of the total protein in the protein bodies of castor bean (Ricinus communis L.), approximately 40% is represented by a group of closely related albumins localized in the matrix of the organelle. This group of albumins has a sedimentation value of 2S and is resolved into several proteins of molecular weight around 12,000 daltons by sodium dodecyl sulfate-acrylamide gel electrophoresis. It has a ...

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ژورنال

عنوان ژورنال: Plant Physiology

سال: 1976

ISSN: 0032-0889,1532-2548

DOI: 10.1104/pp.58.6.703