Analyzing the effects of protecting osmolytes on solute–water interactions by solvatochromic comparison method: II. Globular proteins

RSC Advances ◽  
2015 ◽  
Vol 5 (73) ◽  
pp. 59780-59791 ◽  
Author(s):  
Luisa A. Ferreira ◽  
Xiao Fan ◽  
Pedro P. Madeira ◽  
Lukasz Kurgan ◽  
Vladimir N. Uversky ◽  
...  

Partitioning of 11 globular proteins was examined in aqueous dextran–PEG–sodium/potassium phosphate buffer (0.01 M K/NaPB, pH 7.4) two-phase systems (ATPSs) containing 0.5 M sorbitol.

2015 ◽  
Vol 50 (9) ◽  
pp. 1459-1467 ◽  
Author(s):  
Ranyere L. Souza ◽  
Rafaella A. Lima ◽  
João A.P. Coutinho ◽  
Cleide M.F. Soares ◽  
Álvaro S. Lima

2007 ◽  
Vol 859 (2) ◽  
pp. 222-228 ◽  
Author(s):  
Georgina Bassani ◽  
Beatriz Farruggia ◽  
Bibiana Nerli ◽  
Diana Romanini ◽  
Guillermo Picó

2016 ◽  
Vol 2 (1) ◽  
pp. 557-560 ◽  
Author(s):  
Steffen Lüers ◽  
Markus Laub ◽  
Herbert P. Jennissen

AbstractUltrahydrophilic titanium miniplates with sandblasted and acid etched (SLA) surfaces were protected from loss of hydrophilicity by an exsiccation layer of salt and stored in a dry state. Various salts in different concentrations were tested in respect to their conservation capacity and optical appearance. Potassium phosphate buffer in a specified composition appeared to be optimal. This optimal system was applied in a long time storage experiment showing no loss of hydrophilicity over years. It was also transferred with success to hyperhydrophilic dental implants.


Blood ◽  
1974 ◽  
Vol 43 (2) ◽  
pp. 239-242 ◽  
Author(s):  
David Kabat

Abstract A procedure is described for visualization of normal and mutant adult hemoglobins in human blood smears. After extraction of blood smears with a concentrated potassium phosphate buffer (2.76 M, pH 7.2), erythrocytes that had adult hemoglobins stained bright red with erythrosin, whereas cells that had only fetal hemoglobin appeared as clear ghosts. Analyses of cord blood from newborn infants indicate that, although most erythrocytes contain only Hb F and a few contain only Hb A, many contain both hemoglobins A and F.


1981 ◽  
Vol 27 (6) ◽  
pp. 627-632 ◽  
Author(s):  
A. Hurst ◽  
A. Hughes

Sublethal heating of Staphylococcus aureus S6 in potassium phosphate buffer caused loss of salt tolerance, D-alanine, and magnesium. During incubation in rich complex media all three of the damaged sites were repaired. Repair occurred more slowly but went to completion in a dilute synthetic medium (DSM), free of D-ala. DSM plus penicillin or D-cycloserine allowed repair of salt tolerance but recovery of normal levels of D-ala or Mg was prevented. When DSM-repaired cells were cultured into fresh rich medium they grew rapidly after a short lag. Cells which had acquired their salt tolerance in DSM plus cycloserine and were D-ala and Mg deficient grew slowly and had a lag of 3 h. We suggest that heat damage has two separate primary targets in S. aureus cells: the membrane, which is manifested by loss of salt tolerance, and a second site, possibly teichoic acids, manifested by loss of D-ala and Mg.


1969 ◽  
Vol 114 (2) ◽  
pp. 331-337 ◽  
Author(s):  
A. S. Shetty ◽  
G. W. Miller

1. δ-Aminolaevulate dehydratase (EC 4.2.1.24) was purified 80-fold from tobacco leaves and its properties were studied. 2. The enzyme had optimum pH7·4 in potassium phosphate buffer, Km6·25×10−4m at 37° and pH7·4, optimum temperature 45° and an activation energy of 11100 cal./mole. 3. The enzyme lost activity when prepared in the absence of cysteine, and this activity was only partly restored by the later addition of thiols. Reagents for thiol groups inactivated the enzyme. 4. Mg2+ was essential for activity, and EDTA and Fe2+ were inhibitory; Mn2+ was an activator or an inhibitor depending on the concentration.


1989 ◽  
Vol 256 (1) ◽  
pp. G67-G71
Author(s):  
Y. Amuro ◽  
W. Yamade ◽  
K. Kudo ◽  
T. Yamamoto ◽  
T. Hada ◽  
...  

The formation of chenodeoxycholic and ursodeoxycholic acids from 7-ketolithocholic acid by human liver preparations was examined in vitro. Liver preparations were incubated with 7-ketolithocholic acid at pH 5.5 in a sodium-potassium-phosphate buffer containing NADPH or NADH. The products formed were analyzed by gas chromatography and gas chromatography-mass spectrometry. Results showed that chenodeoxycholic and ursodeoxycholic acids could be formed from 7-ketolithocholic acid by human liver enzyme(s). The enzyme(s) required NADPH but not NADH as coenzyme and was localized largely in the microsomes. The conjugated 7-ketolithocholic acid, especially the taurine conjugated, was predominantly reduced to chenodeoxycholic acid, whereas the unconjugated 7-ketolithocholic acid was not reduced well to either chenodeoxycholic acid or ursodeoxycholic acid. Thus the reduction of 7-ketolithocholic acid by human liver enzyme(s) was found to be dependent on whether the substrate was conjugated or not.


1991 ◽  
Vol 5 (1) ◽  
pp. 82-86 ◽  
Author(s):  
Donald J. Daigle ◽  
Peter J. Cotty

The influences of pH, surfactants, and nutrients on germination were investigated to develop a basis for improvement ofAlternaria cassiaemycoherbicide formulations. In vitro results indicated that a formulation with a pH of approximately 6.5 containing 0.1 to 1% Tween 80, 0.02 M potassium phosphate buffer, and 1% dehydrated potato dextrose broth best promoted germination. Sicklepod plants at the 2 to 3 true-leaf stage were sprayed with test solutions, incubated in the dark at 100% relative humidity (28 C) for 6 h, and placed in a growth chamber maintained at 30 C. Assessment of the plants after 2 d indicated that the ability of the formulation components to induce germination ofAlternaria cassiaein vitro corresponded well with their ability to improve infection of sicklepod seedlings.


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