Probing different conformational states of bovine .alpha.-lactalbumin: fluorescence studies with 5,5'-bis[8-anilino-1-naphthalenesulfonate]
- 1 July 1985
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 24 (15) , 3852-3856
- https://doi.org/10.1021/bi00336a006
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 9 references indexed in Scilit:
- 4,4'-Bis[8-(phenylamino)naphthalene-1-sulfonate] binding to human thrombins: a sensitive exo site fluorescent affinity probeBiochemistry, 1985
- Metal-ion-dependent hydrophobic-interaction chromatography of α-lactalbuminsAnalytical Biochemistry, 1984
- The lactose synthase acceptor site: a structural map derived from acceptor studiesMolecular and Cellular Biochemistry, 1984
- A distinct zinc-binding site in the .alpha.-lactalbumins regulates calcium binding. Is there a physiological role for this control?Biochemistry, 1983
- Metal ion binding to .alpha.-lactalbumin speciesBiochemistry, 1982
- Binding of naphthalene dyes to the N and A conformers of bovine α-lactalbuminArchives of Biochemistry and Biophysics, 1982
- BINDING OF CA2+ IONS TO BOVINE ALPHA-LACTALBUMIN - STUDY BY MEANS OF INTRINSIC PROTEIN FLUORESCENCE CHANGES1982
- Preparation, crystalline structure, and spectral properties of the fluorescent probe 4,4'-bis-1-phenylamino-8-naphthalenesulfonateJournal of the American Chemical Society, 1978
- Immobilized bovine lactose synthase A method of topographical analysis of the active siteBiochimica et Biophysica Acta (BBA) - Enzymology, 1978