FLUORESCENCE KINETICS OF COMPLEX FORMATION BETWEEN HUMAN SERUM ALBUMIN AND ZINC-PHTHALOCYANINE TETRASULFONIC ACID.
Stopped-flow fluorescence was employed to measure the dissociation constant, activation energy, and frequency factor for zinc phthalocyanine tetrasulfonic acid binding to human serum albumin. A pseudo 1storder "Isolation Method" was used to measure temperature dependent rate constants at pH 7.00. Binding was followed by a relatively large emission signal that indicated the formation of a protein-ligand complex. The dissociation constant, activation energy and frequency factor were 3.3 (±0.3)×10-5(M), 4.5 (±0.2)×104J/mol, and 1.1 (±0.1)×108min-1respectively.
Department of Natural Science & Mathematics, Chemistry Program, Savannah State University, Savannah, GA 31404.
Cecil L
CL
Jones
Althea
A
Fields
Lana
L
Thomas
Shreya
S
Patel
Shanice
S
Biggins
Isolation Method; Photodynamic therapy; Stopped-flow fluorescence; Zinc phthalocyanine