DIFFERENTIATION BETWEEN TRYPTOPHAN RESIDUES IN PROTEINS

被引：29

作者：

ELKANA, Y

机构：

[1] Graduate Department of Biochemistry, Brandeis University, Waltham

[2] Department of Biophysics, Weizmann Institute of Science, Rehovoth

来源：

JOURNAL OF PHYSICAL CHEMISTRY | 1968年 / 72卷 / 10期

关键词：

D O I：

10.1021/j100856a050

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The heterogeneity of emitting tryptophans in proteins is investigated by fluorescence measurements. Electronic-excitation energy transfer from the tryptophans in lysozyme, bovine serum albumin, human serum albumin, and a lysozyme-inhibitor complex to an external acceptor in the solution is illustrated. From the shift in the fluorescence spectrum of the tryptophans in the proteins upon addition of an acceptor, it is shown that there are at least two kinds of emitting tryptophans. A kinetic treatment based on a model of two emitting species shows that the dependence of the fluorescence intensity at different parts of the spectrum on the acceptor concentration should be different. This conclusion is verified experimentally.

引用

页码：3654 / &