Red Emitting VCSEL

Jetter, Michael; Roßbach, R.; Michler, Peter

doi:10.1007/978-3-642-24986-0_12

Cited by 2 publications

(1 citation statement)

References 65 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A flow rate of 14 mL/h was performed and fractions of 3 mL were collected and monitored at 280 nm. Affinity column was constructed by immobilizing vanillic acid on Sepharose 4B gel as described by Jetter (2014) …”

Section: Methodsmentioning

confidence: 99%

Purification and characterization of a platelet aggregation inhibitor and anticoagulant Cc 5_NTase, CD 73‐like, from Cerastes cerastes venom

Saoud

Chérifi

Benhassine

et al. 2016

J Biochem & Molecular Tox

View full text Add to dashboard Cite

The present study is the first attempt to report the characterization of a nucleotidase from Cerastes cerastes venom. A 70 kDa 5'-nucleotidase (Cc-5'NTase) was purified to homogeneity. The amino acid sequence of Cc-5'NTase displayed high homology with many nucleotidases. Its activity was optimal at pH 7 with a specific hydrolytic activity toward mono-, di-, and triphosphate adenylated nucleotides. Cc-5'NTase preferentially hydrolyzed ADP and obeyed Michaelis-Menten kinetics. Among the metals and inhibitors tested, Ni and Mg completely potentiated enzyme activity, whereas EGTA, PMSF, iodoacetamide, vanillic acid, vanillyl mandelic acid, and 1,10-phenanthroline partially abolished its activity. Cc-5'NTase was not lethal for mice at 5 mg/kg and exhibited in vivo anticoagulant effect. It also dose-dependently inhibited adenosine diphosphate-induced platelet aggregation by converting adenosine diphosphate to adenosine and prohibited arachidonic acid-induced aggregation but was not effective on fibrinogen-induced aggregation. Cc-5'NTase could be a good tool as pharmacological molecule in thrombosis diagnostic and/or therapy.

show abstract

Section: Methodsmentioning

confidence: 99%