Anonymous ID: 4ea3ff Oct. 10, 2018, 12:05 p.m. No.3426919   🗄️.is 🔗kun

25-Jul-2018 C182 Aurora Muni (KARR) General Mitchell Intl (KMKE) 10:44AM CDT 11:26AM CDT 0:41

24-Jul-2018 C182 Fond Du Lac County (KFLD) Aurora Muni (KARR) 04:33PM CDT 05:28PM CDT 0:54

 

you can't carry the plane.. so why so meticulous about logging in ith a fgt plan but every now and then not filing one?

Anonymous ID: 4ea3ff JFKJR seial no Oct. 10, 2018, 12:07 p.m. No.3426946   🗄️.is 🔗kun

18265525 serial no plane jfkjrof

 

search it get this :

 

Evidence for the presence and role of tightly bound adenine nucleotides in phospholipid-free purified Micrococcus lysodeikticus adenosine triphosphatase.

Muñoz C1, Palacios P, Muñoz E.

Author information

Abstract

[32P]-labeled ATPase was isolated in a highly purified state from Micrococcus lysodeikticus strain PNB grown in medium supplemented with [32P]orthophosphate. Selective extraction procedures allowed us to determine that at least 25% of the firmly bound label belonged to adenine nucleotides, ATP and ADP being present in equimolar amounts. However, no 32P label was found to be part of phospholipids. This was confirmed by purification of the ATPase from cells fed with [2-3H]glycerol. Using the>luciferin-luciferase<< assay we estimated that ATPase freshly isolated by Sephadex chromatography (specific activity 10-14 micromole substrate transformed x min(-1) x mg protein(-1)) contained 2 moles ATP/mole of enzyme. The ratio fell with the age of enzyme and its purification by gel electrophoresis and this was paralleled by a loss of ATPase activity. The endogenous nucleotides were readily exchanged by added ADP or ATP. This result suggests that the sites for tight binding of adenine nucleotides are equivalent, although ADP seems to have a higher affinity for them. The last properties represent a peculiar characteristic of this bacterial ATPase as compared with other bacterial and organelle energy-transducing proteins.

 

PMID: 18265525