Lymphocyte stimulation in vitro by proteinases and its augmentation with a proteinase binding factor from human skin.

J Eskola; J E Fräki

doi:10.1007/bf00446444

Home/Archive/PubMed

PubMed · 736607

Lymphocyte stimulation in vitro by proteinases and its augmentation with a proteinase binding factor from human skin.

J Eskola·J E Fräki

View original source ↗Export metadata ↓

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

Enzyme Inhibitors Humans Lymphocyte Activation Peptide Hydrolases Protein Binding Skin Trypsin Journal Article

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

J Eskola, J E Fräki. 1978-11-10. Lymphocyte stimulation in vitro by proteinases and its augmentation with a proteinase binding factor from human skin.. https://doi.org/10.1007/bf00446444

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

KEEP EXPLORING

Related citations

PubMed2007

Slow-binding inhibition of soybean lipoxygenase-1 by dodecyl gallate.

Dodecyl gallate inhibited the soybean lipoxygenase-1 (EC 1.13.11.12, type-1) catalyzed peroxidation of linoleic acid with an IC50 of 0.007 microM without being oxidized. The progress curves for enzyme reactions were recorded by both spectrophotometric and polarographic methods, and the inhibition kinetics revealed competitive and slow-binding inhibition. Both the initial velocity and steady-state rate in the progress curve decreased with increasing dodecyl gallate. The kinetic parameters that described the inhibition by dodecyl gallate were evaluated by nonlinear regression fits.

Enzyme Inhibitors↗

PubMed2007

Rediscovery of the susceptibility of G6PD deficient persons to methemoglobinemia from oxidant drugs, and to hemolysis from methylene blue.

Explore the source record for details and available documents.

Enzyme Inhibitors↗

PubMed2006

Modeling zinc enzyme inhibition with functional thiolate ligands.

The blocking of zinc enzymes by thiolate-containing inhibitors was modeled by treating TpPh,MeZn-OH with functional thiols. The latter were chosen such that they contain an additional donor function (COOH, COOR, NH2, NHR, OH) in a position favorable for chelation. Of them, mercapto carboxylic acid esters were incorporated as thiolates. The corresponding mercapto carboxylic acids, however, used only their carboxylate function for coordination. Various mercapto amines, mercapto alcohols, and mercaptophenol were exclusively converted to thiolate ligands. The two modes of inhibitor attachment, terminal or chelating, were observed equally frequently. As a rule, they occur as alternatives for similar ligands. In case of 2-mercaptophenol they coexist in the crystalline state and in solution. Hydrogen bonding, both intra- and intermolecular, seems to be a decisive factor determining the inhibitor attachments. Its persistence in solution is underlined by the observation that TpPh,MeZn-hydroxythiophenolates are methylated about 2 orders of magnitude slower than TpPh,MeZn-SPh itself.

Enzyme Inhibitors↗