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Titolo:
Mutational analysis of sickle haemoglobin (Hb) gelation
Autore:
Li, XF; Himanen, JP; de Llano, JJM; Padovan, JC; Chait, BT; Manning, JM;
Indirizzi:
Northeastern Univ, Dept Biol, Boston, MA 02115 USA Northeastern Univ Boston MA USA 02115 iv, Dept Biol, Boston, MA 02115 USA Mem Sloan Kettering Canc Ctr, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr New York NY USA 10021 New York, NY 10021 USA Fdn Valenciana Invest Biomed, Inst Invest Citol, Valencia 46010, Spain FdnValenciana Invest Biomed Valencia Spain 46010 Valencia 46010, Spain Rockefeller021iv, Lab Mass Spectrometry & Gaseous Ion Chem, New York, NY 10 Rockefeller Univ New York NY USA 10021 Gaseous Ion Chem, New York, NY 10
Titolo Testata:
BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
, volume: 29, anno: 1999,
parte:, 2
pagine: 165 - 184
SICI:
0885-4513(199904)29:<165:MAOSH(>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECOMBINANT HUMAN HEMOGLOBIN; TRANSGENIC MOUSE MODEL; INTERMOLECULAR CONTACTS; FUNCTIONAL-PROPERTIES; OXYGEN-AFFINITY; CELL-ANEMIA; POLYMERIZATION; YEAST; SITE; MUTANT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Manning, JM Northeastern5Univ, Dept Biol, Mugar 414,360 Huntington Ave, Boston, MA 0211 Northeastern Univ Mugar 414,360 Huntington Ave Boston MA USA 02115
Citazione:
X.F. Li et al., "Mutational analysis of sickle haemoglobin (Hb) gelation", BIOT APP B, 29, 1999, pp. 165-184

Abstract

The use of recombinant Hb has provided the advantage that any amino acid substitution can be made at sites not represented by natural mutants or thatcannot be modified by chemical procedures, We have recently reported the expression of human sickle Hb (HbS) in the yeast Saccharomycescerevisiae that carries a plasmid containing the human alpha- and beta-globin cDNA sequences; N-terminal nascent protein processing is correct and a soluble correctly folded Hb tetramer is produced. The yeast system produces a recombinant sickle Hb that is identical by about a dozen biochemical and physiological criteria with the natural sickle Hb purified from the red cells of sickle-cell anaemia patients. Most importantly, the gelling concentration of this recombinant sickle Hb is the same as that of the HbS purified from human sickle red cells, The misfolding of Hb reported for the Escherichia coli-expressed protein is not apparent for Hb expressed in yeast by any of the criteria that we have used for characterization. These findings indicate that this system is well suited to the production of HbS mutants to explore those areas of the HbS tetramer whose roles in the gelation process are not yet defined and to measure quantitatively the strength of such interactions at certain inter-tetrameric contact sites in the deoxy-HbS aggregate. This article reviews our studies on a number of sickle Hb mutants, including polymerization-enhancing HbS mutants and polymerization-inhibiting HbS mutants.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 22:41:39