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Titolo:
THE DIMER-TETRAMER EQUILIBRIUM OF RECOMBINANT HEMOGLOBINS - STABILIZATION OF THE ALPHA(1)BETA(2) INTERFACE BY THE MUTATION BETA(CYS112-]GLY) AT THE ALPHA(1)BETA(1) INTERFACE
Autore:
FRONTICELLI C; GATTONI M; LU AL; BRINIGAR WS; BUCCI JLG; CHIANCONE E;
Indirizzi:
UNIV MARYLAND,SCH MED,DEPT BIOCHEM,108 N GREENE ST BALTIMORE MD 21201 UNIV ROME,CNR,CTR MOLEC BIOL,DEPT BIOCHEM SCI A ROSSI FANELLI I-00185ROME ITALY TEMPLE UNIV,DEPT CHEM PHILADELPHIA PA 19122
Titolo Testata:
Biophysical chemistry
fascicolo: 1, volume: 51, anno: 1994,
pagine: 53 - 57
SICI:
0301-4622(1994)51:1<53:TDEORH>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; EXPRESSION; COOPERATIVITY; SITE;
Keywords:
RECOMBINANT HEMOGLOBIN; SUBUNIT ASSEMBLY; DIFFERENTIAL GEL FILTRATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
13
Recensione:
Indirizzi per estratti:
Citazione:
C. Fronticelli et al., "THE DIMER-TETRAMER EQUILIBRIUM OF RECOMBINANT HEMOGLOBINS - STABILIZATION OF THE ALPHA(1)BETA(2) INTERFACE BY THE MUTATION BETA(CYS112-]GLY) AT THE ALPHA(1)BETA(1) INTERFACE", Biophysical chemistry, 51(1), 1994, pp. 53-57

Abstract

The dimer-tetramer association constants of several recombinant humanhemoglobins (in the CO form) have been measured by differential gel filtration. Recombinant human hemoglobin prepared from recombinant beta-chains, and mutant hemoglobins where the substitution was on the surface, beta(Thr4 --> Asp), in the heme pocket, beta(Val67 --> Thr), at the 2,3-DPG binding site, beta(Val1 --> Met + His2del), had a twofold smaller association with respect to natural hemoglobin. In a mutant at the alpha(1) beta(2) interface, beta(Cys93 --> Ala), the association constant was decreased three-fold. Conversely, in a mutant at the alpha(1) beta(1) interface, beta(Cys112 --> Gly), the association constant was two- and four-fold increased with respect to natural and recombinant human hemoglobin. These differences are energetically very small, consistent with the correct folding of the recombinant hemoglobins. Thestabilization of the tetrameric structure by a mutation at the alpha(1) beta(1) interface indicates that structural changes at this interface can be propagated through the protein to the alpha(1) beta(1) interface and, thereby, exert an effect on the allosteric equilibrium.

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Documento generato il 23/11/20 alle ore 21:37:17