PubMed Health⌕ Search

PubMed · 8435078

Effect of thiol compounds on human complement component C4.

Abstract

Thiol compounds have been investigated as inhibitors of the covalent binding reaction of human complement protein C4 using Sepharose-C1s as a combined activating and binding surface. o- and p-substituted aminothiophenols are equally effective inhibitors, whereas the m-substituted compound is a less potent inhibitor. The anti-hypertensive drug captopril is also shown to inhibit the covalent binding reaction. A comparison of the effects of these compounds on the covalent binding reaction of isolated C4A and C4B has been made. Results suggest that a Pro-to-Leu substitution in C4B is likely to account for the differences in inhibitory potency of C4B compared with C4A observed with the aromatic inhibitors.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

S Edmonds, A Gibb, E Sim. 1993-02-01. Effect of thiol compounds on human complement component C4.. https://doi.org/10.1042/bj2890801

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

A mechanism for oxygen exchange between ligated oxometalloporphinates and bulk water.

Oxygen exchange between high-valent metal-oxo complexes and bulk water has been monitored for nonligated model porphyrins (hemin, FeTDCPPS, MnTMPyP) and the axially ligated microperoxidase-8 (MP-8). Exchange extents up to 90% were measured for MP-8 in spite of the presence of an axial histidine ligand and accompanied by the formation of nonlabelled H(2)O(2) from H(2)(18)O(2). These results point to the existence of a mechanism for oxygen exchange between the high-valent iron-oxo complex and the solvent different from the so-called "oxo-hydroxo tautomerism." Regeneration of the primary oxidant, H(2)O(2), and oxygen exchange by axially ligated porphyrins can be explained by a mechanism involving the reversibility of compound I formation.

Aminophenols↗

Migration behavior and separation of benzenediamines, aminophenols and benzenediols by capillary zone electrophoresis.

The migration behavior and separation of five benzendiamines, five aminophenols and three benzenediols were investigated in capillary zone electrophoresis. The results indicate that benzendiamines and aminophenols are optimally separated with a phosphate buffer at pH 5, whereas benzenediol isomers are best separated at pH about 12. The addition of surfactant monomers of tetradecyltrimethylammonium bromide to a phosphate buffer at pH 5 under the conditions of reversed electroosmotic flow is effective for separating these dye intermediates, except for the separation of 1,2-benzenediol from 1,3-benzenediol. The addition of sodium tetraborate as an electrolyte modifier is effective in the separation of 1,2-benzenediol from 1,3-benzenediol, but the latter comigrates with the 1,4-benzenediol isomer at pH 5.0. The electrophoretic mobility of ionized analytes can be described with Offord's equation, and the migration order depends on their ratios of charge to mass. In addition, the pKa values of these analytes in 50 mM phosphate buffer are reported.

Aminophenols↗

Lipoxygenase-mediated biotransformation of p-aminophenol in the presence of glutathione: possible conjugate formation.

This study tested a hypothesis that soybean lipoxygenase (SLO), a model enzyme, may be capable of generating a glutathione (GSH) conjugate(s) from p-aminophenol (PAP). Horseradish peroxidase was employed as a positive control. GSH depletion or an increase in the absorption at 327 nm with time due to GS-PAP formation was used to quantitate the reaction. The rate of GS-PAP formation was dependent on the incubation time and the amount of SLO and exhibited Km values of 0.44 and 0.71 mM for PAP and H2O2, respectively. Classical inhibitors of lipoxygenase and free radical scavengers markedly decreased the rate of GS-PAP formation in a concentration-dependent manner. PAP-dependent GSH depletion from the reaction medium occurred at a rate of 2.37 +/- 0.18 micromol/min/mg protein. Collectively, the results suggest that lipoxygenase pathway may be involved in the enzymatic formation of GSH conjugate(s) from PAP.

Aminophenols↗