INVESTIGADORES
AÑON Maria Cristina
artículos
Título:
Common molecular features among amaranth storage proteins
Autor/es:
MARTINEZ, E.N; CASTELLANI, O.F; AÑÓN, M.C
Revista:
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Editorial:
AMER CHEMICAL SOC
Referencias:
Año: 1997 vol. 45 p. 3832 - 3839
ISSN:
0021-8561
Resumen:
The structure of albumin 2 protein fraction of amaranth was investigated. It was formed by several
major polypeptide subunits of molecular masses of 52.3 ( 0.8, 54 ( 2, and 56 ( 1 kDa. The former
and the latter subunits were composed of a peptide of molecular mass between 31 and 38 kDa
linked by S-S bonds with another peptide of molecular mass between 19 and 23 kDa. The 54 kDa
subunit together with the 31-38 and 19-23 kDa subunits formed S-S-linked aggregated
polypeptides. Lyophilized albumin 2 was highly polymerized, having a complex monomer component
with a molecular mass of 300 ( 10 kDa. The polymers were partially stabilized by SS linkages.
Because of these structural characteristics, albumin 2 was very similar to amarantin except for the
presence of the 54 kDa subunit and its tendency to polymerize. Two components were obtained by
gel filtration of globulin fraction. The major one exhibited heterogeneity of species and showed
some common features with albumin 2. The minor component eluted at a lower volume and also
showed heterogeneity, with a main species of 7S and a minor one of 12S. Their major peptides had
molecular masses of 78, 72, 39, 30, and 20 kDa similar to the 7S type globulin. Its size, larger than
that of amarantin, is different from a 7S type globulin, but the possibility of becoming polymerized
or having a shape quite different from that of a sphere cannot be dismissed.( 0.8, 54 ( 2, and 56 ( 1 kDa. The former
and the latter subunits were composed of a peptide of molecular mass between 31 and 38 kDa
linked by S-S bonds with another peptide of molecular mass between 19 and 23 kDa. The 54 kDa
subunit together with the 31-38 and 19-23 kDa subunits formed S-S-linked aggregated
polypeptides. Lyophilized albumin 2 was highly polymerized, having a complex monomer component
with a molecular mass of 300 ( 10 kDa. The polymers were partially stabilized by SS linkages.
Because of these structural characteristics, albumin 2 was very similar to amarantin except for the
presence of the 54 kDa subunit and its tendency to polymerize. Two components were obtained by
gel filtration of globulin fraction. The major one exhibited heterogeneity of species and showed
some common features with albumin 2. The minor component eluted at a lower volume and also
showed heterogeneity, with a main species of 7S and a minor one of 12S. Their major peptides had
molecular masses of 78, 72, 39, 30, and 20 kDa similar to the 7S type globulin. Its size, larger than
that of amarantin, is different from a 7S type globulin, but the possibility of becoming polymerized
or having a shape quite different from that of a sphere cannot be dismissed.-S bonds with another peptide of molecular mass between 19 and 23 kDa. The 54 kDa
subunit together with the 31-38 and 19-23 kDa subunits formed S-S-linked aggregated
polypeptides. Lyophilized albumin 2 was highly polymerized, having a complex monomer component
with a molecular mass of 300 ( 10 kDa. The polymers were partially stabilized by SS linkages.
Because of these structural characteristics, albumin 2 was very similar to amarantin except for the
presence of the 54 kDa subunit and its tendency to polymerize. Two components were obtained by
gel filtration of globulin fraction. The major one exhibited heterogeneity of species and showed
some common features with albumin 2. The minor component eluted at a lower volume and also
showed heterogeneity, with a main species of 7S and a minor one of 12S. Their major peptides had
molecular masses of 78, 72, 39, 30, and 20 kDa similar to the 7S type globulin. Its size, larger than
that of amarantin, is different from a 7S type globulin, but the possibility of becoming polymerized
or having a shape quite different from that of a sphere cannot be dismissed.-38 and 19-23 kDa subunits formed S-S-linked aggregated
polypeptides. Lyophilized albumin 2 was highly polymerized, having a complex monomer component
with a molecular mass of 300 ( 10 kDa. The polymers were partially stabilized by SS linkages.
Because of these structural characteristics, albumin 2 was very similar to amarantin except for the
presence of the 54 kDa subunit and its tendency to polymerize. Two components were obtained by
gel filtration of globulin fraction. The major one exhibited heterogeneity of species and showed
some common features with albumin 2. The minor component eluted at a lower volume and also
showed heterogeneity, with a main species of 7S and a minor one of 12S. Their major peptides had
molecular masses of 78, 72, 39, 30, and 20 kDa similar to the 7S type globulin. Its size, larger than
that of amarantin, is different from a 7S type globulin, but the possibility of becoming polymerized
or having a shape quite different from that of a sphere cannot be dismissed.( 10 kDa. The polymers were partially stabilized by SS linkages.
Because of these structural characteristics, albumin 2 was very similar to amarantin except for the
presence of the 54 kDa subunit and its tendency to polymerize. Two components were obtained by
gel filtration of globulin fraction. The major one exhibited heterogeneity of species and showed
some common features with albumin 2. The minor component eluted at a lower volume and also
showed heterogeneity, with a main species of 7S and a minor one of 12S. Their major peptides had
molecular masses of 78, 72, 39, 30, and 20 kDa similar to the 7S type globulin. Its size, larger than
that of amarantin, is different from a 7S type globulin, but the possibility of becoming polymerized
or having a shape quite different from that of a sphere cannot be dismissed.