Isolation and Characterization of Protein Bodies From Developing Wheat Endosperm

Graham, Janet Sd; Morton, R. K.; Raison, JK

doi:10.1071/bi9630375

Cited by 35 publications

(34 citation statements)

References 1 publication

(1 reference statement)

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“…It has been known for many years More recently there have been attempts to isolate these particles from wheat (7,10,13) from groundnut (1, 2) from pea (18) and from cotton seed (20) by using differential sedimentation in a variety of media. The reported composition always includes a predominance of protein, justifying the name of protein body.…”

mentioning

confidence: 99%

Protein Bodies of the Soybean

Tombs

1967

Plant Physiol.

116

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mentioning

confidence: 99%

Protein Bodies of the Soybean

Tombs

1967

Plant Physiol.

116

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“…It also explains why, after repeated extractions with pyrophosphate buffer, proteins usually extracted by this solvent are detected in dilute acetic acid extracts Graham, Morton, and Raison 1963). This relationship also casts doubt on the assumption of Graham, Morton, and Raison (1964) that the proteins which migrated in gels in region 1 in their pyrophosphate extracts and high-speed supernatant fractions are cytoplasmic proteins.…”

Section: Discussionmentioning

confidence: 83%

“…These protein bodies had an amino acid composition rather similar to that of the proteins extracted by dilute alkali from the same preparation of endosperm (Jennings and Morton 1963c). Graham, Morton, and Raison (1963) and Morton, Raison, and Smeaton (1964) also found that their protein body preparations contained significant amounts of proteins which were soluble in pyrophosphate buffer.…”

Section: Discussionmentioning

confidence: 89%

“…Some of the results obtained by and Graham, Morton, and Raison (1964), while studying the incorporation of amino acids labelled with radioactive isotopes into endosperm proteins, also appear to support this conclusion. Graham, Morton, and Raison (1963) concluded that the incorporation of amino acids into their "high-speed supernatant" fraction (or proteins extracted by pyrophosphate buffer) preceded that into the small "protein bodies". These protein bodies had an amino acid composition rather similar to that of the proteins extracted by dilute alkali from the same preparation of endosperm (Jennings and Morton 1963c).…”

Section: Discussionmentioning

confidence: 99%

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The Characterization by Electrophoresis of the Proteins Extracted by Dilute Alkali From Wheat Flour

Jennings¹

1968

Aust. Jnl. Of Bio. Sci.

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SummaryProcedures have been developed for characterizing, in a chemically unaltered form, the proteins usually extracted in dilute alkali from wheat flour or endosperm.The electrophoretic zone patterns of the proteins migrating to the cathode in this fraction were qualitatively identical with those of a previously described high·speed supernatant fraction of wheat endosperm. In addition, there was a slow movement of proteins to the anode.Intermolecular disulphide bonds do not appear to be present in flour or formed during the preparation of a dough.It is concluded that most of the proteins previously considered to be of cytoplasmic origin are storage proteins. The following mechanism is proposed for the formation, in developing endosperm, of the protein fraction extracted by alkali. The proteins soluble in pyrophosphate buffer are neutralized by proteins, or other compounds, with a net negative charge at physiological pH values and which are synthesized in stoichiometric amounts. These complexes may then interact mainly through hydrophobic bonds to form aggregates insoluble in dilute aqueous buffers and dilute acids.It is concluded that there are two types of storage proteins, synthesized by separate systems. One type is characterized, in gel electrophoresis, by relatively low mobilities, the other by relatively high mobilities.

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“…Coates and Simmonds (1961) have also isolated protein fractions from wheat flour which have a relatively high arginine content although the studies of Graham, Morton, and Raison (1963), Jennings and Morton (1963), and Morton, Palk, and Raison (1964) have not indicated that endosperm protein bodies are rich in arginine.…”

Section: Introductionmentioning

confidence: 99%

Localization of Arginine-Rich Proteins in Mature Seeds of some Members of the Gramineae

Fulcher¹,

O’Brien²,

Simmonds³

1972

Aust. Jnl. Of Bio. Sci.

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Several mature grass seeds (Triticum aestivum L., Avena sativa L., Andropogon sorghum Brot., Echinochloa utilis Ohwi & Yabuno, and Lolium perenne L.) were fixed and embedded in glycol methacrylate. Thin (1-2 p.m) sections were examined by light microscopy after staining specifically for arginine residues or basic proteins. The aleurone protein bodies of all seeds stained intensely by these methods but there was considerable variation in concentration and organization of the argininerich basic proteins in endosperm tissue of the various seeds. Amino acid analysis was used to confirm the histochemical differences in basic amino acid concentration between the aleurone layer and endosperm of T. aBstivum.

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Isolation and Characterization of Protein Bodies From Developing Wheat Endosperm

Cited by 35 publications

References 1 publication

Protein Bodies of the Soybean

Protein Bodies of the Soybean

The Characterization by Electrophoresis of the Proteins Extracted by Dilute Alkali From Wheat Flour

Localization of Arginine-Rich Proteins in Mature Seeds of some Members of the Gramineae

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