INVESTIGADORES
AÑON Maria Cristina
artículos
Título:
Role of Disulfide Bonds upon the Structural Stability of an
Autor/es:
CASTELLANI, F.O; MARTINEZ, N.E; AÑON, M.C
Revista:
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Editorial:
AMER CHEMICAL SOC
Referencias:
Año: 1999 vol. 47 p. 3001 - 3008
ISSN:
0021-8561
Resumen:
Analysis of globulin-P, the polymerized amaranth globulin, gave a low amount of free sulfhydryls
(10.2 ( 0.5 ímol/g) from which 7 ( 1 ímol/g was buried inside the molecule. In addition, its disulfide
content was high (51 ( 1 ímol/g) and similar to soybean 11S globulin content. The more exposed
disulfide bridges were found to be stabilizing polymers, whereas the less reactive bridges were either
linking P20 and P30 polypeptides or forming intrachain linkages. It was found that the buried bonds
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
disulfide bridges were found to be stabilizing polymers, whereas the less reactive bridges were either
linking P20 and P30 polypeptides or forming intrachain linkages. It was found that the buried bonds
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
content was high (51 ( 1 ímol/g) and similar to soybean 11S globulin content. The more exposed
disulfide bridges were found to be stabilizing polymers, whereas the less reactive bridges were either
linking P20 and P30 polypeptides or forming intrachain linkages. It was found that the buried bonds
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
disulfide bridges were found to be stabilizing polymers, whereas the less reactive bridges were either
linking P20 and P30 polypeptides or forming intrachain linkages. It was found that the buried bonds
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
( 0.5 ímol/g) from which 7 ( 1 ímol/g was buried inside the molecule. In addition, its disulfide
content was high (51 ( 1 ímol/g) and similar to soybean 11S globulin content. The more exposed
disulfide bridges were found to be stabilizing polymers, whereas the less reactive bridges were either
linking P20 and P30 polypeptides or forming intrachain linkages. It was found that the buried bonds
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
disulfide bridges were found to be stabilizing polymers, whereas the less reactive bridges were either
linking P20 and P30 polypeptides or forming intrachain linkages. It was found that the buried bonds
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
( 1 ímol/g) and similar to soybean 11S globulin content. The more exposed
disulfide bridges were found to be stabilizing polymers, whereas the less reactive bridges were either
linking P20 and P30 polypeptides or forming intrachain linkages. It was found that the buried bonds
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences
20 and P30 polypeptides or forming intrachain linkages. It was found that the buried bonds
participate in the stabilization of folded polypeptides and the quaternary structure of the globulin.
In turn, the dissociation of polymers and disruption of the quaternary structure by the action of
2-mercaptoethanol reverted upon removal of the reducing agent. This demonstrates that the
polymerized state and the quaternary structure of the molecules are most favorable from the
thermodynamic point of view. The similar content of SH and SS in globulin-P and globulin-S found
in this laboratory suggests that the differences between these proteins may be ascribed to other
compositional differences