EFFECTS OF NEUTRAL SALTS ON THERMAL-STABILITY OF SPINACH FERREDOXIN

被引:12
作者
HASUMI, H
NAKAMURA, S
KOGA, K
YOSHIZUMI, H
机构
[1] KITASATO UNIV,SCH MED,DEPT BIOPHYS CHEM,SAGAMIHARA,KANAGAWA 228,JAPAN
[2] SUNTORY CENT RES INST,MISHIMA,OSAKA 618,JAPAN
关键词
D O I
10.1016/S0006-291X(79)80020-0
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 effects of various neutral salts on the thermal stability of spinach ferredoxin were studied by means of differential scanning calorimetry and circular dichroism. Upon addition of 1 M NaCl, the apparent denaturation temperature increased by about 13°, and the enthalpy and activation energy for the denaturation also increased by 27% and 44%, respectively. The salt effect was ascribed essentially to the ionic strength of the environment. The circular dichroism measurements showed that the interaction between the iron-sulfur cluster and the protein moiety was modulated by the salt, resulting in stabilization of the protein, It is therefore highly probable that the native ferredoxin structure is maintained through the interaction with the iron-sulfur chromophore. © 1979 Academic Press, Inc. All rights of reproduction in any form reserved.
引用
收藏
页码:1095 / 1101
页数:7
相关论文
共 13 条
[1]  
DONOVAN JW, 1975, J BIOL CHEM, V250, P1966
[2]   INCREASE IN STABILITY OF AVIDIN PRODUCED BY BINDING OF BIOTIN - DIFFERENTIAL SCANNING CALORIMETRIC STUDY OF DENATURATION BY HEAT [J].
DONOVAN, JW ;
ROSS, KD .
BIOCHEMISTRY, 1973, 12 (03) :512-517
[3]  
DONOVAN JW, 1975, J BIOL CHEM, V250, P6026
[4]  
DONOVAN JW, 1975, J BIOL CHEM, V250, P6022
[5]  
HASUMI H, 1978, J BIOCHEM-TOKYO, V84, P707, DOI 10.1093/oxfordjournals.jbchem.a132176
[6]  
HIPPEL PH, 1969, STRUCTURE STABILITY, P417
[7]  
KERESZTESNAGY S, 1966, J BIOL CHEM, V241, P5955
[8]  
MATSUBARA H, 1976, IRON COPPER PROTEINS, V74, P1
[9]  
PADMANAB.R, 1970, J BIOL CHEM, V245, P2469
[10]  
PETERING D, 1971, J BIOL CHEM, V246, P643