Micronization of water-soluble or alcohol-soluble pharmaceuticals and model compounds with a low-temperature Bubble Dryer®

2003 ◽  
Vol 26 (1) ◽  
pp. 9-16 ◽  
Author(s):  
R.E. Sievers ◽  
E.T.S. Huang ◽  
J.A. Villa ◽  
G. Engling ◽  
P.R. Brauer
2019 ◽  
Vol 33 (2) ◽  
pp. 1527-1539 ◽  
Author(s):  
Jin-liang Li ◽  
Wei Lu ◽  
Biao Kong ◽  
Ying-jiazi Cao ◽  
Guan-sheng Qi ◽  
...  

1990 ◽  
Vol 270 (2) ◽  
pp. 413-417 ◽  
Author(s):  
M J Berry ◽  
S J George ◽  
A J Thomson ◽  
H Santos ◽  
D L Turner

Cytochrome c″ (Methylophilus methylotrophus) is a soluble protein, Mr 15,000, possessing one haem which is high-spin in the reduced state but switches to a low-spin form on oxidation. Low-temperature electron-paramagnetic-resonance spectroscopy of the oxidized state shows a low-spin signal at gz = 3.65 with a folded line-shape typical of a haem of low rhombicity, and the near-infrared magnetic-circular-dichroism (m.c.d.) spectra reveal an unusually intense (delta epsilon = 400 M-1.cm-1 at 5 T, 4.2 K) charge-transfer band at 1560 nm, establishing that the oxidized haem is co-ordinated by two His residues in a near-perpendicular orientation. This conformation is well established for transmembrane b cytochromes, but this appears to be the first example in a water-soluble cytochrome. The low-temperature m.c.d. spectra of the reduced form of the protein confirms that the haem contains a high-spin Fe2+ ligated by one His residue. The redox-linked spin-state change releases a His group. Since this residue is likely to bind a proton at pH values less than 6.5, this cytochrome may provide a useful model of a molecular mechanism of a redox-linked proton uptake and release process.


2013 ◽  
Vol 56 ◽  
pp. 111-119 ◽  
Author(s):  
Matt J. Norwood ◽  
Patrick Louchouarn ◽  
Li-Jung Kuo ◽  
Omar R. Harvey

Holzforschung ◽  
1983 ◽  
Vol 37 (4) ◽  
pp. 199-204 ◽  
Author(s):  
Robert Brežný ◽  
Vincent Mihalov ◽  
Vladimír Kováčik

2015 ◽  
Vol 114 (19) ◽  
Author(s):  
G. Reményi ◽  
S. Sahling ◽  
K. Biljaković ◽  
D. Starešinić ◽  
J.-C. Lasjaunias ◽  
...  

2011 ◽  
Vol 1326 ◽  
Author(s):  
L. Shannon Davis ◽  
Thomas T. Eisenhart ◽  
Brianna C. Hughes ◽  
Amy L. Pressley

ABSTRACTOxidation catalysis is a reaction necessary for the production of plastics and other materials that seem now essential to our everyday lives. Unfortunately, most oxidation processes suffer from poor selectivity or yields, creating unwanted byproducts and waste. In nature, oxidative enzymes like methane monooxygenase and the family of cytochromes provide a more selective method for oxidation of organic compounds. Of particular interest is the low temperature, selective oxidation of cellulosic biomass for the production of biofuels or other useful replacements for materials currently derived from petroleum feedstocks. An enzymatic approach could replace the high temperature pyrolysis technology in use today. A series of inorganic mimics of some oxidative enzymes, using transition metal – amino acid complexes encapsulated in large pore zeolites have been synthesized and examined as oxidation catalysts under benign conditions. Several of these demonstrate turnovers comparable to native enzymes in the reaction of model compounds for the oxidation of lignin and cellulose.


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