English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The inhibitory effect of D-penicillamine on the denaturation of human gamma-globulin induced by heat and Cu++ was compared with the action of other agents such as antirheumatic drugs, anti-inflammatory drugs, SH reagents, SH inhibitors and chelating reagents. The denaturation of human gamma globulin was induced by Cu++ at 10 micrometer ("Cu++ induced denaturation") and was further increased by heating at 63 degrees C for 3 hr in the presence of Cu++ ("total denaturation"). Thus the value obtained by subtracting "Cu++ induced denaturation" from "total one" was designated as "thermal denaturation". D-Penicillamine enhanced "thermal denaturation" at a low concentration but inhibited it with increasing the concentration as well as L-cysteine. SH reagents such as thiomalic acid, 6-mercaptopurine inhibited "total" and "thermal" denaturation. SH inhibitors and protein binding reagents such as N-ethylmaleimide, trinitrobenzenesulfonic acid inhibited the "total" and "thermal" denaturation of the protein. Chelating reagents such as ethylenediamine tetraacetic acid, 8-hydroxyquinoline inhibited "total", "Cu++ induced" and "thermal" denaturation of the protein. Au+ inhibited "total denaturation", but not "Cu++ induced denaturation". On the other hand, Au+++ denaturated the protein considerably with or without heating, in the absence of Cu++ but dithiothreitol did so only with heating in the same condition. The anti-inflammatory drugs used herein had no effect on the protein denaturation. D-Penicillamine apparently prevents the denaturation of human gamma-globulin by the chelate formation with Cu++ and the binding to free protein SH, initiator for sulfhydryldisulfide interchange reaction.

Studies on D-penicillamine (1): Inhibitory effect of D-penicillamine on the heat-Cu++ induced denaturation of human 7-globulin.