Interaction of alcohols with proteins

Biopolymers - Tập 17 Số 9 - Trang 2121-2131 - 1978
Henry B. Bull1, Keith Breese1
1Department of Biochemistry, University of Iowa, Iowa City, Iowa 52242

Tóm tắt

AbstractThe kinetics of denaturation of egg albumin have been determined for methanol, ethanol, propanol, and butanol. The reactions are first order in respect to protein but between 11th and 18th order for the alcohols. The denaturation reaction is characterized by a large temperature coefficient with little or no dependence on pH. There is a marked change of pH when proteins are denatured. A series of eight proteins has been studied. There is surprisingly little difference in susceptibility to alcohol denaturation between the various proteins. Methanol, ethanol, propanol, and butanol are strongly bound to egg albumin—butanol being the most strongly bound. The binding of alcohol is probably accompanied by protein dehydration. The polyhydric alcohols' behavior is much different. These alcohols do not denature proteins and the protein is hydrated. Sucrose produces the greatest degree of hydration.

Từ khóa


Tài liệu tham khảo

10.1016/S0065-3233(08)60051-0

10.1016/S0021-9258(18)63111-4

10.1111/j.1432-1033.1970.tb00272.x

10.1002/bip.1975.360141015

10.1002/bip.1976.360150811

10.1042/bj0300227

10.1016/0003-9861(73)90311-1

Bianchi E., 1970, J. Biol. Chem., 245, 3341, 10.1016/S0021-9258(18)63001-7

10.1016/0022-0248(68)90071-7

10.1021/bi00676a001

Gibbs J. W., 1928, Collected Works.

10.1021/ja00995a036

Noelken M. E., 1967, J. Biol. Chem., 242, 5080, 10.1016/S0021-9258(18)99478-0

10.1021/bi00699a005

10.1016/0003-9861(70)90443-1

10.1016/0003-9861(70)90049-4

10.1016/0003-9861(67)90243-3

10.1016/0003-9861(67)90244-5

10.1021/bi00671a005

Thông tin
Thông tin xuất bản

Biopolymers

Tập 17 Số 9

2121-2131

Thông tin tác giả