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PMID: 1238119 Published · ppublish English Journal Article

The structure, physical and chemical properties of the soy bean protein glycinin.

Biochimica et biophysica acta ·Vol. 412 ·No. 2 ·1975-12-15 ·Pages 214-28

Badley RA, Atkinson D, Hauser H, Oldani D, Green JP, Stubb JM

Abstract

The major storage protein of the soybean, glycinin, has been prepared in a homogeneous form and examined by a variety of techniques. It has been found that the protein has a molecular weight of 320000 and contains two sizes of subunits with different isoelectric points. There are six acidic subunits of approximately 35000 and six basic of approximately 20000. Analysis revealed three different kinds of acidic subunits and probably three kinds of basic ones also. These twelve subunits are packed in two identical hexagons, placed one on the other, yielding a hollow oblate cylinder of 110 X 110 X 75 A. Some or all of the subunits are non-spherical resulting in a partial blocking of the central hole. Information about the forces stabilzing the native structure is also discussed.

MeSH Terms
Amino Acids/analysis Globulins Macromolecular Substances Microscopy, Electron Molecular Weight Plant Proteins/analysis,isolation & purification Protein Conformation Scattering, Radiation Soybean Proteins Soybeans/analysis Viscosity
Chemicals
Amino Acids Globulins Macromolecular Substances Plant Proteins Soybean Proteins glycinin
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Badley R A
Atkinson D
Hauser H
Oldani D
Green J P
Stubb J M
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1975-12-15
Pages
214-28
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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