IN VITRO BINDING OF PROPRANOLOL AND PROGESTERONE TO NATIVE AND DESIALYLATED HUMAN OROSOMUCOID

Authors
  1. Wong, A.K.L.
  2. Hsia, J.C.
Corporate Authors
Defence and Civil Inst of Environmental Medicine, Downsview ONT (CAN)
Abstract
A comparison of propranolol and progesterone binding to native and desialylated human orosomucoid was studied by means of equilibrium dialysis. The association constants of propranolol and progesterone binding to native human orosomucoid under physiological conditions were 8.4 X E5 and 3.2 X E5 M1(-), respectively. Enzymatic desialylation of human orosomucoid removed 95% of the sialic acid content and reduced the binding affinity of propranolol from 8.4 X E5 to 6.0 X E5 M1(-), but the affinity of progesterone was not affected. In addition, desialylation reduced the percent binding for propranolol, indicating that electrostatic attraction of the positive charge on propranolol by sialic acid residues on human orosomucoid had some effect on the binding ability of purified orosomucoid for propranolol. TRUNCATED
Report Number
83-P-35 — Research Paper
Date of publication
01 Jan 1983
Number of Pages
3
Reprinted from
Can J of Biochemistry and Cell Biology, vol 61, no 10, 1983, p 1114-1116
DSTKIM No
84-02681
CANDIS No
122034
Format(s):
Microfiche filmed at DSIS;Originator's fiche received by DSIS;Hardcopy

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