A Comparison of Soybean Globulins and the Protein Bodies in the Protein Composition

Ikunori KOSHIYAMA

doi:10.1271/bbb1961.36.62

A Comparison of Soybean Globulins and the Protein Bodies in the Protein Composition

Agricultural and Biological Chemistry ◽

10.1271/bbb1961.36.62 ◽

1972 ◽

Vol 36 (1) ◽

pp. 62-67 ◽

Cited By ~ 8

Author(s):

Ikunori KOSHIYAMA

Keyword(s):

Protein Composition ◽

Protein Bodies ◽

Soybean Globulins

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A Comparison of Soybean Globulins and the Protein Bodies in the Protein Composition

Agricultural and Biological Chemistry ◽

10.1080/00021369.1972.10860211 ◽

1972 ◽

Vol 36 (1) ◽

pp. 62-67 ◽

Cited By ~ 7

Author(s):

Ikunori Koshiyama

Keyword(s):

Protein Composition ◽

Protein Bodies ◽

Soybean Globulins

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Ultrastructure of protein bodies in mutant rice (Oryza sativa L.) with altered storage protein composition

Breeding Science ◽

10.1270/jsbbs.61.201 ◽

2011 ◽

Vol 61 (2) ◽

pp. 201-207 ◽

Cited By ~ 6

Author(s):

Kanae Ashida ◽

Yuhi Saito ◽

Takehiro Masumura ◽

Shuichi Iida

Keyword(s):

Oryza Sativa ◽

Storage Protein ◽

Oryza Sativa L ◽

Protein Composition ◽

Protein Bodies

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Where is the prolamine located in rice endosperm?

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100161035 ◽

1990 ◽

Vol 48 (3) ◽

pp. 696-697

Author(s):

Hsin-Kan Wu ◽

Mei-Chu Chung

Keyword(s):

Storage Protein ◽

Sodium Phosphate ◽

Recent Experiment ◽

Protein A ◽

Uranyl Acetate ◽

Protein Bodies ◽

Lead Citrate ◽

Thin Sections ◽

Rice Endosperm ◽

Ethanol Series

In one of our earlier papers (Wu et al. 1978), we suggested that glutelin is the major composition of the round storage protein bodies although they also contain relatively more prolamine than the angular one does. Immunochemical studies of Krishnan et al. (1986) later showed the presence of glutelin in the irregularly-shaped (angular) protein bodies while the prolamines were found in the round ones. Our recent experiment using protein A-gold technique found that prolamine is mainly deposited into the angular protein bodies.Small blocks (1 mm3) of 7 DAF (days after flowering) caryopsis of Orvza perennis were fixed with 3% paraformaldehyde and 3% glutaraldehyde in 0.1M sodium phosphate, pH7.4, dehydrated in a graded ethanol series and infiltrated with Spurr’s resin. Thin sections, after gold labeling, were stained with uranyl acetate and lead citrate. Rabbit antibodies were raised against purified prolamine. Protein A-gold sol complex was prepared based on the technique of Horisberger et al. (1977).

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Bovine Platelet Proteins

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653555 ◽

1969 ◽

Vol 21 (03) ◽

pp. 409-418 ◽

Cited By ~ 2

Author(s):

S Łopaciuk ◽

N. O Solum

Keyword(s):

Bovine Serum ◽

Protein Composition ◽

Disc Electrophoresis ◽

Plasma Fibrinogen ◽

Plasma Albumin ◽

Precipitin Line ◽

Bovine Plasma ◽

Platelet Proteins

Summary1. The protein composition of bovine platelet extracts has been investigated by immunoelectrophoresis and polyacrylamide disc electrophoresis. The information obtained is discussed as a basis for study on platelet fibrinogen.2. With antiserum to platelet proteins 11 precipitin lines were observed 3 of which corresponded electrophoretically to plasma albumin, fibrinogen and γ-globulin. These lines were not seen using the same antiserum absorbed with bovine plasma. The 8 additional lines were still present indicating that they represented specific platelet components. Antiserum to plasma produced the 3 above-mentioned lines, but no others.3. With antiserum to purified bovine plasma fibrinogen 3 precipitin lines were observed. The fibrinogen line was the dominant one. The 2 additional lines did not disappear by absorption of the antiserum with bovine serum nor by incubation of the extracts with thrombin. The latter treatment totally removed the fibrinogen line.4. A non-fibrinogen precipitin line, observed only with the antiserum to platelet extract and positioned in the β2-globulin region, disappeared by the incubation of platelet extracts with thrombin.

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