Optical Waveguide Fabrication by Stoichiometric Implantation of Ti and O into LiNbO3

1989 ◽  
Vol 157 ◽  
Author(s):  
D. B. Pokers ◽  
W. Xia
Keyword(s):  
Phase Separation ◽  
Optical Waveguides ◽  
Room Temperature ◽  
High Substrate Temperature ◽  
The Stability ◽  
Waveguide Fabrication ◽  
Water Saturated ◽  
Substrate Annealing ◽  
Planar Optical Waveguides ◽  
Saturated Oxygen

ABSTRACTX-cut substrates of LiNbO3 have been implanted at 500°C with Ti and O to doses of 2.5 and 7.5×l017 ions/cm2, respectively. The high substrate temperature during implantation ensures dynamic recrystallization, preserving the crystallinity of the LiNbOs-The stability of the stoichiometric implants is enhanced sufficiently that annealing at 1000°C proceeds with no surface degradation of the substrate. Annealing under identical conditions without the 0 implant usually results in phase separation of an oxide at the surface, even when annealing is performed immediately following implantation. Samples implanted with Ti and O to preserve the stoichiometric metahoxygen ratio of the substrate can be stored at room temperature for several months without phase separation. Planar optical waveguides have been produced by stoichiometric implantation followed by annealing in water-saturated oxygen for one hour at temperatures of 900 and 1000°C. The sample annealed at 900°C supported a single lossy mode, while the 1000°C sample supported two propagating modes and one lossy mode at λ=0.6μm.

Solid-phase epitaxy of Ti-implanted LiNbO3

1989 ◽  
Vol 4 (2) ◽  
pp. 412-416 ◽  
Author(s):  
D. B. Poker ◽  
D. K. Thomas
Keyword(s):  
Optical Waveguides ◽  
Solid Phase ◽  
Complete Removal ◽  
Amorphous Region ◽  
Liquid Nitrogen Temperature ◽  
High Dose ◽  
Solid Phase Epitaxy ◽  
Complete Recrystallization ◽  
Water Saturated ◽  
Saturated Oxygen

The solid-phase epitaxy of LiNbO3 following ion implantation of Ti dopant for the purpose of producing optical waveguides has been studied. Implanting 360-keV Ti at liquid nitrogen temperature produces a highly damaged region extending to a depth of about 400 nm. This essentially amorphous region can be recrystallized epitaxially by annealing in a water-saturated oxygen atmosphere at temperatures near 400 °C. though complete removal of all irradiation-induced damage requires temperatures in excess of 600 °C. The activation energy of the regrowth is 2.0 eV for implanted fluences below 3 ⊠ 1016 Ti/cm2. At higher fluences the regrowth proceeds more slowly, and Ti dopant segregates at the regrowth interface. Complete recrystallization following high-dose implantation requires annealing temperatures in excess of 800 °C.

scholarly journals FORMULATION AND EVALUATION OF RED PALM OLEIN NANOEMULSION

2018 ◽  
Vol 11 (9) ◽  
pp. 237
Author(s):  
Febia Sari ◽  
Kasmirul Ramlan Sinaga ◽  
Donald Siahaan
Keyword(s):  
Particle Size ◽  
Phase Separation ◽  
Room Temperature ◽  
Palm Olein ◽  
Tween 80 ◽  
Size Measurement ◽  
Spontaneous Emulsification ◽  
Particle Size Measurement ◽  
The Stability ◽  
Red Palm Olein

Objective: The objective of this study is to formulate and evaluate the red palm olein (RPO) nanoemulsion using spontaneous emulsification method.Methods: Nanoemulsion formulated by spontaneous emulsification method using the comparison of surfactant (tween 80) and cosurfactant (sorbitol) concentration with the variation of RPO concentration. Evaluation of the stability of the nanoemulsion preparation includes centrifugation test, viscosity, pH, organoleptic observation (odor, color, clarity, and phase separation), and particle size measurement during 12 weeks storage at room temperature.Result: The results showed that all nanoemulsion preparations were transparent yellow, characteristic odor, type weights 1.0166–1.0641 g/ml, and stable for 12 weeks storage at room temperature. The smallest particle size was produced by the nanoemulsion preparation in a formula of the concentration of 5%, which was 67, 64 nm.Conclusion: RPO can be formulated as a nanoemulsion by spontaneous emulsification method. RPO with a 5% concentration is very stable for 12 weeks storage.

Solid-phase epitaxy of ion-implanted LiNbO3 for optical waveguide fabrication

1987 ◽  
Vol 2 (2) ◽  
pp. 222-230 ◽  
Author(s):  
Ch. Buchal ◽  
P. R. Ashley ◽  
B. R. Appleton
Keyword(s):  
Optical Waveguides ◽  
Solid Phase ◽  
Surface Region ◽  
Liquid Nitrogen Temperature ◽  
High Concentration ◽  
Near Surface ◽  
Crystalline Substrate ◽  
A New Technique ◽  
Waveguide Fabrication ◽  
Water Saturated

A new technique for successfully fabricating high-quality optical waveguides in LiNbO3 is reported. A high concentration of Ti is implanted with the substrate at liquid nitrogen temperature and an amorphous, Ti-rich, nonequilibrium phase is produced in the implanted, near-surface region. Subsequent thermal annealing in water-saturated oxygen atmosphere at up to 1000°C initiates solid-phase epitaxial regrowth onto the crystalline substrate. A highquality single crystalline layer results that is rich in Ti and has excellent waveguiding properties.

Methods for the Concentration of Bovine Ac-Globulin (Factor V)

1961 ◽  
Vol 06 (03) ◽  
pp. 435-444 ◽  
Author(s):  
Ricardo H. Landaburu ◽  
Walter H. Seegers
Keyword(s):  
Room Temperature ◽  
Barium Carbonate ◽  
Deae Cellulose ◽  
Reducing Agents ◽  
Factor V ◽  
Isoelectric Precipitation ◽  
Stabilizing Agent ◽  
Bovine Plasma ◽  
The Stability

SummaryAn attempt was made to obtain Ac-globulin from bovine plasma. The concentrates contain mostly protein, and phosphorus is also present. The stability characteristics vary from one preparation to another, but in general there was no loss before 1 month in a deep freeze or before 1 week in an icebox, or before 5 hours at room temperature. Reducing agents destroy the activity rapidly. S-acetylmercaptosuccinic anhydride is an effective stabilizing agent. Greatest stability was at pH 6.0.In the purification bovine plasma is adsorbed with barium carbonate and diluted 6-fold with water. Protein is removed at pH 6.0 and the Ac-globulin is precipitated at pH 5.0. Rivanol and alcohol fractionation is followed by chromatography on Amberlite IRC-50 or DEAE-cellulose. The final product is obtained by isoelectric precipitation.

Tyrosine-Selective Bioconjugation with Iminoxyl Radicals

2020 ◽  
Author(s):  
Katsuya Maruyama ◽  
Takashi Ishiyama ◽  
Yohei Seki ◽  
Kounosuke Oisaki ◽  
Motomu Kanai
Keyword(s):  
Reaction Time ◽  
Steric Hindrance ◽  
Room Temperature ◽  
Water Soluble ◽  
Light Irradiation ◽  
Sodium Ascorbate ◽  
Iminoxyl Radical ◽  
Short Reaction Time ◽  
Modified Peptides ◽  
The Stability

A novel Tyr-selective protein bioconjugation using the water-soluble persistent iminoxyl radical is described. The conjugation proceeded with high Tyr-selectivity and short reaction time under biocompatible conditions (room temperature in buffered media under air). The stability of the conjugates was tunable depending on the steric hindrance of iminoxyl. The presence of sodium ascorbate and/or light irradiation promoted traceless deconjugation, restoring the native Tyr structure. The method is applied to the synthesis of a protein-dye conjugate and further derivatization to azobenzene-modified peptides.

Circular dichroism and infrared study of β-turn formation in repeat peptides of elastin

1987 ◽  
Vol 52 (5) ◽  
pp. 1356-1361
Author(s):  
S. Abdel Rahman ◽  
M. Elsafty ◽  
A. Hattaba
Keyword(s):  
Circular Dichroism ◽  
Solid State ◽  
Ir Spectra ◽  
Chain Length ◽  
Room Temperature ◽  
Infrared Study ◽  
Feature Characteristic ◽  
C 50 ◽  
The Stability ◽  
Circular Dichroïsm

The conformation of elastin-like peptides Boc-Ala-Pro-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Ala-Pro-Gly-Val-Gly-Val-APEGM, Boc-Ala-Pro-Gly-Val-Gly-Val-Ala-Pro-Gly-Val-Gly-Val-APEGM were examined in solution using circular dichroism at 30 °C, 50 °C, and 70 °C and in solid state by IR at room temperature. The studies show that the β-turn is a significant conformational feature for peptides under investigation in solution at 30 °C and 50 °C, but at 70 °C the tetra, hexa, and decapeptides show the CD feature characteristic of the β-structure while the dodecapeptide spectra show the presence of β-turn which indicates the stability of the β-turn at this chain length. The IR spectra show that in the solid state at room temperature all investigated peptides assume essentially a β-turn except the tetrapeptide which present evidence of antiparallel β-structure. The β-turn contribution in the IR spectra increases with the increase of the chain length of the peptide.

Cholesterol in Serum and Lipoprotein Fractions

1956 ◽  
Vol 2 (3) ◽  
pp. 145-159 ◽  
Author(s):  
Joseph T Anderson ◽  
Ancel Keys
Keyword(s):  
Human Serum ◽  
Total Cholesterol ◽  
Filter Paper ◽  
Room Temperature ◽  
Paper Electrophoresis ◽  
Cholesterol Content ◽  
Intraindividual Variability ◽  
Detailed Data ◽  
The Stability ◽  
Source Of Error

Abstract 1. Methods are described for the separation, by paper electrophoresis and by cold ethanol, of α- and β-lipoproteins in 0.1 ml. of serum, with subsequent analysis of cholesterol in the separated portions. 2. It is shown that both methods of separation yield separated fractions containing substantially the same amounts of cholesterol. 3. Detailed data are given on the errors of measurement for total cholesterol and for cholesterol in the separated lipoprotein fractions. 4. Studies are reported on the stability of cholesterol in stored serum and on paper electrophoresis strips. It is shown that simple drying on filter paper causes no change in cholesterol content and yields a product that is stable for many weeks at ordinary room temperature. 5. The sources of variability in human serum cholesterol values are examined and it is shown that spontaneous intraindividual variability is a much greater source of error than the errors of measurement with these methods.

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