Tags

Type your tag names separated by a space and hit enter

Interactions of chlorphenesin and divalent metal ions with phosphodiesterase.
Arch Int Pharmacodyn Ther. 1976 Sep; 223(1):24-33.AI

Abstract

Chlorphenesin inhibition of the hydrolysis of cyclic AMP by guinea-pig lung phosphodiesterase was reversed by the addition of exogenous magnesium ions. Chlorphenesin and theophylline inhibition of this enzyme was shown to be noncompetitive when the substrate concentration was low. Kinetic studies of the inhibition of beef heart phosphodiesterase by chlorphenesin and theophylline indicated that the substrate concentration was a factor in determining whether inhibition was competitive or noncompetitive. Calcium, cobalt and copper ions were inhibitory to guinea-pig lung phosphodiesterase. The inhibition due to chlorphenesin was partially reversed by low (40 mM or less) concentrations of barium ions; high concentrations of barium ions, or manganese ions, were inhibitory. The concentration of the divalent cation did not affect the type of inhibition that was observed.

Authors

No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

187130

Citation

Edelson, J, and J P. McMullen. "Interactions of Chlorphenesin and Divalent Metal Ions With Phosphodiesterase." Archives Internationales De Pharmacodynamie Et De Therapie, vol. 223, no. 1, 1976, pp. 24-33.
Edelson J, McMullen JP. Interactions of chlorphenesin and divalent metal ions with phosphodiesterase. Arch Int Pharmacodyn Ther. 1976;223(1):24-33.
Edelson, J., & McMullen, J. P. (1976). Interactions of chlorphenesin and divalent metal ions with phosphodiesterase. Archives Internationales De Pharmacodynamie Et De Therapie, 223(1), 24-33.
Edelson J, McMullen JP. Interactions of Chlorphenesin and Divalent Metal Ions With Phosphodiesterase. Arch Int Pharmacodyn Ther. 1976;223(1):24-33. PubMed PMID: 187130.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Interactions of chlorphenesin and divalent metal ions with phosphodiesterase. AU - Edelson,J, AU - McMullen,J P, PY - 1976/9/1/pubmed PY - 1976/9/1/medline PY - 1976/9/1/entrez SP - 24 EP - 33 JF - Archives internationales de pharmacodynamie et de therapie JO - Arch Int Pharmacodyn Ther VL - 223 IS - 1 N2 - Chlorphenesin inhibition of the hydrolysis of cyclic AMP by guinea-pig lung phosphodiesterase was reversed by the addition of exogenous magnesium ions. Chlorphenesin and theophylline inhibition of this enzyme was shown to be noncompetitive when the substrate concentration was low. Kinetic studies of the inhibition of beef heart phosphodiesterase by chlorphenesin and theophylline indicated that the substrate concentration was a factor in determining whether inhibition was competitive or noncompetitive. Calcium, cobalt and copper ions were inhibitory to guinea-pig lung phosphodiesterase. The inhibition due to chlorphenesin was partially reversed by low (40 mM or less) concentrations of barium ions; high concentrations of barium ions, or manganese ions, were inhibitory. The concentration of the divalent cation did not affect the type of inhibition that was observed. SN - 0003-9780 UR - https://www.unboundmedicine.com/medline/citation/187130/Interactions_of_chlorphenesin_and_divalent_metal_ions_with_phosphodiesterase_ DB - PRIME DP - Unbound Medicine ER -