Tris-glycine buffer v1

protocols.io ◽  
2016 ◽  
Author(s):  
Stanton Burnton
Keyword(s):  
Glycine Buffer

scholarly journals Optical Properties of Crystalline Lactose Fluidized with Dilutions of Various Substances in the Terahertz Frequency Range

Pharmaceutics ◽  
2021 ◽  
Vol 14 (1) ◽  
pp. 32
Author(s):  
Anna Baranova ◽  
Anastasiya Lykina ◽  
Daria Antonova ◽  
Olga Smolyanskaya
Keyword(s):  
Optical Properties ◽  
Interferon Gamma ◽  
Fluidized Beds ◽  
Principal Component ◽  
Terahertz Frequency ◽  
Frequency Range ◽  
Terahertz Time Domain Spectroscopy ◽  
Terahertz Frequency Range ◽  
Glycine Buffer ◽  
Diluted Solution

Lactose is a commonly used component of pharmaceutical medications in tablet form. It was previously shown that lactose changes conformationally after saturation in fluidized beds with active pharmaceutical ingredients obtained by repeated dilution of antibodies to interferon-gamma in combination with an external intensive vibration treatment. Moreover, it was revealed that these solutions are self-organized dispersed systems in which nano-objects are formed. Their biological activity and mechanism of action were previously established as well. The current work was dedicated to investigating the optical properties of fluidized lactose powders in the terahertz frequency range. Spectral analyses of powders of crystalline lactose saturated in fluidized beds with a diluted solution of either glycine buffer, antibodies to interferon-gamma, or water were carried out, intact lactose served as a control. All powders were tableted before testing. In the course of the study, the macroscopic parameters of the tablets were established, at which they had a stable shape and their THz optical properties had no parasitic diffraction losses. These tablets were analyzed using terahertz time-domain spectroscopy in the frequency range of 0.2–2.6 THz. The differentiation between the spectra was conducted using a principal component analysis. The differences between intact lactose and the lactose saturated with any of studied solutions were demonstrated. Additionally, lactose saturated with solutions of multiple dilutions of a substance (antibodies or glycine buffer) differed not only from intact lactose, but also from lactose saturated with a diluted solution of water. Moreover, discrimination of lactose formulations saturated with different substances (antibodies or glycine buffer) was also possible. Additionally, intact lactose differed from lactose saturated with diluted water. The methods reported could be useful for the quality control of the medications based on the technology of repeated dilution of an original substance.

DOSE REGIMENS OF HUMAN GROWTH HORMONE: EFFECTS OF CONTINUOUS INFUSION AND OF A GELATIN VEHICLE ON GROWTH IN RATS AND RATE OF ABSORPTION IN RABBITS

1980 ◽  
Vol 87 (2) ◽  
pp. 303-312 ◽  
Author(s):  
P. MARY COTES ◽  
W. A. BARTLETT ◽  
ROSE E. GAINES DAS ◽  
P. FLECKNELL ◽  
R. TERMEER
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Plasma Levels ◽  
Time Course ◽  
Human Growth ◽  
Daily Injection ◽  
Glycine Buffer ◽  
Hormone Effects ◽  
Rate Of Absorption ◽  
Hypophysectomized Rats

Different methods for administration of human growth hormone (hGH) have been examined with a view to efficient use of the limited amounts of hGH at present available for clinical use. We found that in hypophysectomized rats (1) hGH administered by continuous subcutaneous infusion induced a greater increase in body weight (referred to throughout as growth) than hGH administered by intermittent (daily) injection and (2) intermittent injections of hGH dissolved in 16% gelatin induced more growth than hGH dissolved in a glycine buffer. It was further found that (1) hGH dissolved in 16% gelatin compared with hGH dissolved in a glycine buffer induced lower maximal levels of immunoreactive plasma hGH and between 7 and 9 h after treatment higher plasma levels when injected subcutaneously in rabbits, (2) 125I-labelled hGH added as a tracer to hGH in gelatin was removed more slowly from subcutaneous injection sites in rabbits than 125I-labelled hGH given with hGH in glycine buffer and (3) changes in the ratio of hGH to gelatin had little effect on the time-course of plasma levels of hGH in the rabbit. Addition of the protease inhibitors aprotinin or 6-aminohexanoic acid, to injection of hGH in gelatin or glycine did not induce any consistent increase in plasma levels of hGH.

scholarly journals Keratin Derivatives Extracted From Wool with Alkaline Thioglycollate Solutions

1955 ◽  
Vol 8 (1) ◽  
pp. 97 ◽  
Author(s):  
JM Gillespie ◽  
FG Lennox
Keyword(s):  
Ionic Strength ◽  
Protein Concentration ◽  
Anomalous Behaviour ◽  
Single Peak ◽  
Minor Components ◽  
Thioglycollic Acid ◽  
Merino Wool ◽  
Glycine Buffer ◽  
Initial Ph

In extension of previous work (Gillespie and Lennox 1953), the conditions under which proteins may be extracted from washed Merino wool have been further examined. Approximately 65 per cent. of the wool can be dissolved by a 40-min extraction at 50�C with O�1M thioglycollate at an initial pH of 12� 6. Electrophoresis at pH 11 in thioglycoIlate-glycine buffer indicated the presence of seven minor and one major component, the latter amounting to 41 per cent. of the wool. The minor components can be completely removed from the wool by five 2,O-min extractions with O�1M thioglycollate at an initial pH of 10�5. Extraction of the residue at pH 12�3 yields the major component. This moves as a single peak on electrophoresis between pH 8�0 and 12�0 in the presence of various buffers. It has a mobility of -7�2 X 10-5 cm2 V-I sec- I at a protein concentration of 0�5 per cent. in thioglycollate-glycine buffer of ionic strength O� 22 at pH 11� O. At higher protein concentrations there is anomalous behaviour on the descending boundary and tills can be prevented by increasing the ionic strength or replacing thioglycollic acid with mercapto-ethanol. The ascending pattern is unaltered by these changes or by increased protein concentration.

Glycine buffer

2009 ◽  
Vol 2009 (1) ◽  
pp. pdb.rec11625-pdb.rec11625
Keyword(s):  
Glycine Buffer

Occurrence of Bacteriophages Infecting Bacteroides fragilis and Other Viruses in Polluted Marine Sediments

1989 ◽  
Vol 21 (3) ◽  
pp. 15-19 ◽  
Author(s):  
J. Jofre ◽  
M. Blasi ◽  
A. Bosch ◽  
F. Lucena
Keyword(s):  
Marine Sediments ◽  
Sodium Nitrate ◽  
Coastal Area ◽  
Bacteroides Fragilis ◽  
Alkaline Ph ◽  
Glycine Buffer ◽  
Beef Extract

Numbers of B.fragilis bacteriophages in comparison to coliphages, enteroviruses and rotaviruses were evaluated by different methods in sediments of a coastal area near Barcelona which receives substantial amounts of pollution of domestic origin. Phages infecting B.fragilis should be eluted from sediments prior to their enumeration, in the same way as solid-associated animal viruses have to.Phages infecting B.fragilis were better eluted by glycine buffer at alkaline pH than by a caotropic agent (beef extract-sodium nitrate). Such differences between glycine buffer and sodium nitrate were not evident when enteroviruses and rotaviruses were eluted from sediments. This suggests that elution with glycine buffer is preferable for bacteriophages, while the use of caotropic agents is advisable for animal viruses, because of the simplicity of the methodology. In the studied area, coliphages were the more abundant viruses. Also, B.fragilis phages outnumbered rotaviruses and enteroviruses by a factor of more than ten. The ratios between phages active against B.fragilis and either enteroviruses or rotaviruses in marine sediments were similar to the ratios found in sewage, thus indicating that they have a similar fate.

Partial purification and properties of an L-arabinose dehydrogenase from Azospirillum brasiliense

1983 ◽  
Vol 29 (2) ◽  
pp. 242-246 ◽  
Author(s):  
Norman J. Novick ◽  
Max E. Tyler
Keyword(s):  
Molecular Weight ◽  
Divalent Cation ◽  
Gel Filtration ◽  
Reducing Agent ◽  
Partial Purification ◽  
Ph Optimum ◽  
Glycine Buffer ◽  
Purification And Properties ◽  
Filtration Technique

An L-arabino-aldose dehydrogenase responsible for the oxidation of L-arabinose to L-arabino-γ-lactone has been purified 59-fold from L-arabinose grown cells of Azospirillum brasiliense. The dehydrogenase was found to be specific for substrates with the L-arabino-configuration at carbons 2, 3, and 4. Km values for L-arabinose of 75 and 140 μM were found with NADP and NAD as coenzymes, respectively. The enzyme had a pH optimum of 9.5 in glycine buffer and was stable when heated to 55 °C for 5 min. No enhancement of activity in the presence of any divalent cation or reducing agent tested was found. L-Arabinose dehydrogenase had a molecular weight of 175 000 as measured by the gel filtration technique.

Cell-free synthesis of rat liver zinc-thioneins

1979 ◽  
Vol 57 (7) ◽  
pp. 1030-1035 ◽  
Author(s):  
Choy L. Hew ◽  
Peter E. Penner
Keyword(s):  
Germ Cell ◽  
Rat Liver ◽  
Gel Electrophoresis ◽  
Zinc Sulfate ◽  
Trichloroacetic Acid ◽  
Wheat Germ ◽  
Translation System ◽  
Glycine Buffer ◽  
Free Translation

The induction of rat liver zinc-thioneins mRNA was studied in a wheat germ cell-free translation system. Liver poly A rich polysomal RNA was isolated from rats which had been injected with zinc sulfate 5 h previously. These RNA preparations stimulated the incorporation of [35S]cystine into trichloroacetic acid insoluble proteins when assayed in the cell-free synthetic system. The translation products were characterized by Sephadex G-75 chromatography in 8 M urea – 50 mM β-mercaptoethanol, by disc gel electrophoresis in 4 M urea – Tris–glycine buffer (pH 9.2), and by peptide fingerprinting with pepsin. These results were identical with authentic rat liver zinc-thioneins. The zinc-thioneins mRNA activity in the control rats, however, was minimal. The stimulation in zinc-thioneins synthesis observed in the cell-free synthesis was similar to the increased synthesis of these polypeptides in vivo.

Preliminary Study of the Autoantigens on the Membrane of Erythropoietic Cells of the Patients with BMMNC- Coomb's Test(+) Hemocytopenia

Blood ◽  
2010 ◽  
Vol 116 (21) ◽  
pp. 4435-4435
Author(s):  
Rong Fu ◽  
Hui Liu ◽  
Zonghong Shao ◽  
Jun Wang ◽  
Lijuan Li
Keyword(s):  
Bone Marrow ◽  
Conflicts Of Interest ◽  
Bone Marrow Mononuclear Cell ◽  
Rt Pcr ◽  
Glycine Buffer ◽  
Healthy Donors ◽  
Preliminary Study ◽  
The Relationship ◽  
Epor Expression ◽  
Normal Controls

Abstract Abstract 4435 Objective To observe the relationship between EPO receptor(EPOR) and autoantibodies-IgG/IgM (auto-Ab) on the membrane of erythropoietic cells of the patients with bone marrow mononuclear cell Coomb's (BMMNC-Coomb's) test(+) immuno-related pancytopenia(IRP), and then explore the probable autoantigens of auto-Ab in IRP. Methods 46 newly diagnosed IRP patients (15 with auto-Ab on erythropoietic cells and 31 without auto-Ab on erythropoietic cells) and 18 healthy donors as controls were enrolled in this study. EPOR expression on their nuclear erythrocytes were tested with flow cytometry to observe the relationship between EPOR and auto-Ab; After sorting erythropoietic cells in bone marrow, EPOR mRNA and protein Stat5,P-Stat5 were investigated by RT-PCR and Western blot to observe the production of EPOR and EPO/EPOR signal transduction; Finally, EPOR expression on the membrane were tested again after stripping auto-Ab with glycine buffer. Results (1) EPOR of auto-Ab(+) arm(1.59±0.87)% was significantly lower than that of auto-Ab (-) arm(4.58±4.09)%(P<0.01), and the latter was significantly higher than that of normal controls (2.27±1.76)%(P<0.05); EPOR of IRP patients was negatively correlated with their auto-Ab (r=-0.543,P=0.000) and its regression equation was Y(EPOR)=0.040-0.335X(auto-Ab);(2)EPOR mRNA of auto-Ab(+) arm(0.685±0.136)was significantly higher than that of auto-Ab (-) arm(0.554±0.116)(P<0.01)and normal controls (0.580±0.119)(P<0.05);(3)Protein Stat5 of auto-Ab(+) arm(1.45±0.94) was significantly higher than that of normal controls (0.54±0.36)(P<0.05); While P-Stat5 of auto-Ab(+) arm(0.42±0.18) was significantly lower than that of normal controls (0.85±0.38)(P<0.05); (4) EPOR expression became higher while auto-Ab became lower after stripping with glycine buffer. Conclusion The auto-Ab of some IRP patients might block or competitively inhibit the EPOR on the membrane of erythropoietic cells. EPOR was one of autoantigens in IRP. Disclosures: No relevant conflicts of interest to declare.

scholarly journals The hydroxylation of tyrosine by an enzyme from third-instar larvae of the blowfly Calliphora erythrocephala.

1975 ◽  
Vol 147 (3) ◽  
pp. 565-573 ◽  
Author(s):  
R N Pau ◽  
C Kelly
Keyword(s):  
Phenol Oxidase ◽  
Enzyme Concentration ◽  
Polyacrylamide Gels ◽  
Dihydroxybenzoic Acid ◽  
Calliphora Erythrocephala ◽  
Glycine Buffer ◽  
Hydrogen Donors ◽  
Lag Period ◽  
Tyrosine Concentration ◽  
Third Instar Larvae

1. Two pro-(phenol oxidase) were distinguished when the blood of late-third-instar larvae of Calliphora erythrocephala was electrophoresed in polyacrylamide gels with Tris-glycine buffer, pH 8.3. One pro-(phenol oxidase), after activation by an enzyme readily catalyses the oxidation of both L-tyrosine and L-3,4-dihydroxyphenylalanine (L-dopa). The second enzyme catalyses the oxidation of L-dopa but not of L-tyrosoine. 2. One of the pro-(phenol oxidases) was purified over 2000-fold from homogenates of whole larvae. This enzyme, after activation, catalyses the oxidation of both dopa and tyrosine. On electrophoresis in polyacrylamide gels with Tris-glycine buffer, pH 8.3, it has the same mobility as the enzyme in the blood which catalyses the oxidation of both tyrosine and dopa. 3. The pro-(phenol oxidase)-activating enzyme was purified over 100-fold from homogenates of whole larvae. 4. The oxidation of L-tyrosine, in the presence of the activated purified phenol oxidase, reached a steady maximum rate after a lag period that was directly related to tyrosine concentration and inversely related to enzyme concentration. 5. The effect of the addition of electron donors on the lag period was studied. Dopa, dopamine (3,4-dihydroxyphenethylamine) and 2-amino-4-hydroxy-6,7-dimethyl-5,6,7,8-tetrahydropteridine are the most effective hydrogen donors. 3,4-Dihydroxybenzoic acid, the oxidation of which was not catalysed by the activated pro-(phenol oxidase), did not affect the lag period.

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