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

Platelet membranes isolated by the glycerol lysis technique contain a pyridine nucleotide dependent reductase which can reduce cytochrome c. This reductase is not inhibited by superoxide dismutase. The Km (apparent) for NADH, the preferred cofactor, is 1 μM. The sulfhydryl reagent, parachloromercuribenzoate sulfonate (PCMBS), inhibits but KCN does not. PCMBS inhibition is time dependent. Inhibition of the reductase is also seen with quinacrine HCl (atebrin) and salts (both monovalent and polyvalent). Cytochemical staining with nitroblue tetrazolium has also localized the reductase to the platelet membrane. ADP and collagen induced aggregation in citrated plasma is inhibited by quinacrine HCl while aggregation by the calcium ionophore A23 187 is not. It has recently been reported that aggregation of human platelets by collagen or thrombin cause an increase in the non-superoxide dependent reduction of cytochrome c or nitroblue tetrazolium (Marcus, A. J., et al., J. Clin. Invest. 59, 149, 1977). The quinacrine HCl inhibition studies suggest that a pyridine nucleotide dependent reductase may be involved in one of the steps which trigger aggregation.

Characterization of a Plasma Membrane Bound Pyridine Nucleotide Reductase from Human Platelets