One-step separation of high-purity (6,5) carbon nanotubes by multicolumn gel chromatography

2011 ◽  
Vol 248 (11) ◽  
pp. 2524-2527 ◽  
Author(s):  
Huaping Liu ◽  
Takeshi Tanaka ◽  
Hiromichi Kataura
2018 ◽  
Vol 2 (1) ◽  
pp. 343-350 ◽  
Author(s):  
Jiaming Cui ◽  
Wei Su ◽  
Dehua Yang ◽  
Shilong Li ◽  
Xiaojun Wei ◽  
...  

1971 ◽  
Vol 10 (03) ◽  
pp. 245-251 ◽  
Author(s):  
P. Richards ◽  
W. C. Eckelman

SummaryThe full potential use of technetium has not been achieved despite its ideal physical properties, dosimetry and availability because of the complex preparations required for 99mTc radiopharmaceuticals. One of the goals of our work is to develop techniques for the preparation of high-purity 99mTc compounds which can be easily prepared, ideally by adding pertechnetate to a prepared solution.The use of stannous ion as reducing agent for technetium makes it possible to obtain such one-step, high-purity products. All non-radioactive components can be premixed in a single vial before addition of the radioactive pertechnetate. No final pH adjustment, further chemical manipulation or purification is required.Procedures for two instantly labeled compounds have been developed to date: 99mTc DTPA and 99mTc HSA. The 99mTc DTPA is prepared by adding pertechnetate to a previously prepared solution of stannous ion and CaNa3 DTPA which has been stored at pH 4. The 99mTc HSA is prepared by adding pertechnetate to a solution of stannous ion and HSA. The parametric variations and analytical techniques involved in formulating these procedures are described. It appears that development of kits for other biologically interesting compounds may be possible using similar procedures.


RSC Advances ◽  
2021 ◽  
Vol 11 (40) ◽  
pp. 24772-24786
Author(s):  
Sveta Zhiraslanovna Ozkan ◽  
Galina Petrovna Karpacheva ◽  
Mikhail Nikolaevich Efimov ◽  
Andrey Aleksandrovich Vasilev ◽  
Dmitriy Gennad'evich Muratov ◽  
...  

In a self-organizing system within one stage under IR heating conditions, hybrid nanomaterials are formed with a structure that contains bimetallic Co–Fe particles, free or immobilized on the SWCNT surface, dispersed in the polymer PDPA matrix.


Author(s):  
Jan J Sixma ◽  
Kjell S Sakariassen ◽  
Piet A Bolhuis

The relation between the VWF-A of F VIII-VWF and its multimeric structure was studied in an annular perfusion chamber according to Baumgartner, with a steady flow system. 51Cr-labelled aspirin treated human platelets and human post mortem renal arteries were employed. F VIII-VWF was purified from cryoprecipitate by agarose gel chromatography and radiolabelled by the lactoperoxydase method. The multimeric distribution was determined by SDS-agarose electrophoresis. Five different commercial high purity concentrates contained multimers between 0.5 and 3.5 x 106 mol wt. None of these concentrates had VWF-A at ristocetin cofactor activities (RIC0F-A) of 1.0 u/ml. A low potency concentrate with mul- timers in the same mol wt range had normal VWF-A. Mild reduction (dithioerythritol-DTE ≤ 2mM) caused a shift in , mol wt range from 3.0 - 20.0 × 106 towards 0.5 - 2.0 × 106 with little decrease in RIC0F-A and VWF-A. Reduction with 10 mM DTE produced multimers of 1.5 and 0.5 × 106 without RICOF-A and VWF-A, but binding normally to the vessel wall. The void volume peak of 125I-VIII-VWF was rechromatographed on Sepharose-2B and arbitrarily divided in fractions A: mol wt 8,0 - 18.0 × 106 ;B: mol wt 4.5 - 11.0 × 106 ; and C: mol wt 2.5 - 6.5 × 106 . Binding of 125I-VIII-VWF to the subendothelium was highest for A, intermediate for B and lowest for C. Correction for mean mol wt showed that almost equal numbers of molecules bound from all three fractions. When the quantity of bound VIII-VWF was thus expressed, all fractions had a similar relative VWF-A.These data indicate that high purity concentrates do not correct the bleeding time at normal RICOF-levels, because they lack VWF-A. Multimers of high mol wt normally carry both RICOF-A and VWF-A, but the high mol wt is no absolute requirement. These data are in agreement with the notion that VWF-A resides on a specific polypeptide chain in the molecule.


2012 ◽  
Vol 25 (1) ◽  
pp. 85-93 ◽  
Author(s):  
Veronika Urbanová ◽  
Mathieu Etienne ◽  
Alain Walcarius

Sign in / Sign up

Export Citation Format

Share Document