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Molecular weight and amino acid composition of glycinin subunits
Author(s) -
Catsimpoolas N.,
Kenney J. A.,
Meyer E. W.,
Szuhaj B. F.
Publication year - 1971
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740220905
Subject(s) - valine , phenylalanine , leucine , proline , tyrosine , alanine , amino acid , chemistry , biochemistry , protein subunit , isoelectric focusing , isoelectric point , composition (language) , glutamic acid , gene , enzyme , linguistics , philosophy
Glycinin, the major soyabean globulin, is composed of subunits having molecular weights of about 22,300, and 37,200. On the basis of amino acid analysis, the six submits of glycinin isolated by isoelectric focusing are all different. The ‘acidic’ subunits have higher content of glutamic acid and proline, whereas the ‘basic’ subunits are higher in the hydrophobic amino acids leucine, tyrosine, phenylalanine, valine and alanine.