The Structure and Biosynthesis of Legume Seed Storage Proteins: A Biological Solution to the Storage of Nitrogen in Seeds

Comparative study of the composition and thermal properties of protein isolates prepared from nine Phaseolus vulgaris legume varieties

“…Legumin, with a molecular mass (MM) of 300 to 400 kDa, has six subunits linked by disulfide bonds (Derbyshire, Wright, & Boulter, 1976). Each subunit can be further divided into an acid subunit with a MM around 40 kDa and a basic subunit with a MM of 20 kDa (Boulter & Croy, 1997). In contrast, vicilin is a trimer (MM: about 150-190 kDa), with each subunit having a MM of around 50 kDa (Boulter & Croy, 1997;Hall, McLeester, & Bliss, 1977) and with an absence of disulfide bonds between the subunits (Meng & Ma, 2001a;Tang, 2008).…”

“…Each subunit can be further divided into an acid subunit with a MM around 40 kDa and a basic subunit with a MM of 20 kDa (Boulter & Croy, 1997). In contrast, vicilin is a trimer (MM: about 150-190 kDa), with each subunit having a MM of around 50 kDa (Boulter & Croy, 1997;Hall, McLeester, & Bliss, 1977) and with an absence of disulfide bonds between the subunits (Meng & Ma, 2001a;Tang, 2008). Although extensive studies have been done on legumin and vicilin structures in P. vulgaris, very few studies have reported on specific legumin and vicilin characteristics such as secondary structures and thermal properties.…”

Study of conformation of vicilin from Dolichos lablab and Phaseolus calcaratus by Fourier-transform infrared spectroscopy and differential scanning calorimetry

“…In this study, the vicilin will be used as a model. Vicilin is a trimer with molecular weight (M w ) around 145-190 kDa, containing three either identical or non-identical monomers (M w 50-70 kDa) that are held together by non-covalent forces and are not disulfidebonded since vicilin monomers are typically but not always devoid of cysteine (Bewley & Black, 1994;Boulter & Croy, 1997;Casey, 1999;Pernollet & Mossé, 1983).…”

Modification of Storage Protein Content and Quality in Legume Seeds

“…Numerous papers and authoritative reviews concerning legume storage proteins have appeared in the past three decades (Boulter, 1965;Derbyshire, Wright, and Boulter, 1976;Wright, 1986;Shewry, Napier, and Tatham, 1995;Boulter and Croy, 1997;Vitale and Bollini, 1997) in view of the prominent role played by this heterogenous family of homologous proteins in the fundamental research, nutrition and technology.…”

“…The seeds are not the unique plant tissues where storage proteins can be found (Boulter and Croy, 1997), however cotyledonary cells are certainly specialized to this role and deposit massive amounts of proteins in the storage vacuoles.…”