Consequence of β16 and β112 replacements on the kinetics of hemoglobin assembly

被引:6
作者
Adachi, K
Yang, Y
Joshi, AA
Vasudevan, G
Morris, A
McDonald, MJ
机构
[1] Univ Massachusetts Lowell, Dept Chem, Biochem Program, Lowell, MA 01854 USA
[2] Univ Penn, Childrens Hosp Philadelphia, Sch Med, Div Hematol, Philadelphia, PA 19104 USA
关键词
human recombinant hemoglobin; subunit assembly; association kinetics; spectroscopy; molecular modeling;
D O I
10.1006/bbrc.2001.5962
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The rates of alpha/beta monomer combination of four beta (A) variants (beta 112C --> S, beta 112C --> D, beta 112C --> T, and beta 112C --> V) in the presence and absence of beta 16G --> D (beta (J)) were measured in an attempt to assess the consequences of amino acid substitution at both a surface (beta 16) and an alpha (1)beta (1) interface (beta 112) residue on oxyhemoglobin assembly. Rates of alpha/beta monomer combination determined spectrally in 0.1 M Tris-HCl, 0.1 M NaCl, 1 mM EDTA, pH 7.4, at 21.5 degreesC differed by over 40-fold (22 +/- 2.0 to 0.49 +/- 0.1 X 10(5) M-1 s(-1)), and were in the order: HbA beta 112S = HbJ beta 16D, beta 112S > HbA beta 112D = HbJ beta 16D, beta 112D > HbA > Hb J > HbA beta 112T = HbJ beta 16D, beta 112T > HbJ beta 16D, beta 112V > HbA beta 112V. This extensive kinetic investigation of single/double amino acid-substituted recombinant hemoglobin molecules, in conjunction with molecular modeling studies, has allowed examination of an array of unique alpha/beta subunit interactions and assembly processes. (C) 2001 Academic Press.
引用
收藏
页码:75 / 79
页数:5
相关论文
共 30 条
[1]  
ADACHI K, 1993, J BIOL CHEM, V268, P21650
[2]   Effects of increased anionic charge in the β-globin chain on assembly of hemoglobin in vitro [J].
Adachi, K ;
Yamaguchi, T ;
Pang, J ;
Surrey, S .
BLOOD, 1998, 91 (04) :1438-1445
[3]   PROPERTIES AND INTERACTIONS OF ISOLATED ALPHA AND BETA CHAINS OF HUMAN HAEMOGLOBIN .I. SEDIMENTATION AND ELECTROPHORETIC BEHAVIOUR [J].
BUCCI, E ;
FRONTICE.C ;
CHIANCON.E ;
WYMAN, J ;
ANTONINI, E ;
ROSSIFAN.A .
JOURNAL OF MOLECULAR BIOLOGY, 1965, 12 (01) :183-&
[4]   ELECTROSTATIC INTERACTIONS IN THE ASSEMBLY OF HEMOGLOBIN [J].
BUNN, HF ;
MCDONALD, MJ .
NATURE, 1983, 306 (5942) :498-500
[5]  
Bunn HF., 1986, HEMOGLOBIN MOL GENET
[6]   Soret spectroscopic and molecular graphic analysis of human semi-β-hemoglobin formation [J].
Chiu, FM ;
Vasudevan, G ;
Morris, A ;
McDonald, MJ .
JOURNAL OF PROTEIN CHEMISTRY, 2000, 19 (02) :157-162
[7]  
Creighton T. E., 1992, PROTEIN FOLDING
[8]  
FERMI G, 1981, HAEMOGLOBIN MYOGLOBI, V2, P405
[9]   PROBES OF SUBUNIT ASSEMBLY AND RECONSTITUTION PATHWAYS IN MULTISUBUNIT PROTEINS [J].
FRIEDMAN, FK ;
BEYCHOK, S .
ANNUAL REVIEW OF BIOCHEMISTRY, 1979, 48 :217-250
[10]   Protein modelling for all [J].
Guex, N ;
Diemand, A ;
Peitsch, MC .
TRENDS IN BIOCHEMICAL SCIENCES, 1999, 24 (09) :364-367