Service for Dynamic Scale Removal of Barium Sulfate in Perforation Tunnels

2011 ◽  
Author(s):  
Kevin Scott Harive ◽  
Cam Van Le ◽  
Mohamed Abdel Khalek
Keyword(s):  
Barium Sulfate ◽  
Scale Removal

Case Study: Barium Sulfate Scale Removal by Dynamic Underbalance

2020 ◽  
Author(s):  
Walid Mohamed Mahmud ◽  
Mansur Ermila
Keyword(s):  
Barium Sulfate ◽  
Scale Removal

Case Histories of Barium Sulfate Scale Removal in Offshore Wells, Brazil, Using a New Engineered Combination of Coiled-Tubing Tools

2007 ◽  
Author(s):  
Zacarias Guimaraes ◽  
Alessandro Barreto Franca ◽  
Luis Humberto Duque ◽  
Rogerio Barreto de Souza ◽  
Marcos Porto ◽  
...  
Keyword(s):  
Barium Sulfate ◽  
Case Histories ◽  
Scale Removal ◽  
Coiled Tubing

Investigations on the Nature of Hemophilia A

1963 ◽  
Vol 09 (01) ◽  
pp. 030-052 ◽  
Author(s):  
Eberhard Mammen
Keyword(s):  
Factor Viii ◽  
Human Plasma ◽  
Barium Sulfate ◽  
Freeze Drying ◽  
Room Temperature ◽  
Hemophilia A ◽  
Normal Human Plasma ◽  
Normal Human ◽  
And Storage ◽  
Prothrombin Activation

SummaryIn this paper an inhibitor is described that is found in hemophilic plasma and serum different from any till now described inhibitor. The inhibitor only inhibits prothrombin activation in the “intrinsic clotting systems”. This inhibitor is probably not present in normal human plasma or serum. It is destroyed by ether and freeze drying, is labile to acid and storage at room temperature. It is stable upon dialysis and has not been adsorbed on barium sulfate, aluminum hydroxide or kaolin. It precipitates at 50% v/v saturation with alcohol. The nature of this inhibitor seems to be a protein or lipoprotein.Factor VIII was isolated from hemophilic plasma. The amount isolated was the same as from normal plasma and the activity properties were not different. Hemophiliacs have normal amounts of factor VIII.

“In vitro” Neutralization with Oxalate Ion of the Anticoagulant Effect of Heparin

1961 ◽  
Vol 05 (02) ◽  
pp. 314-318 ◽  
Author(s):  
W. O Cruz ◽  
L Meis ◽  
C. P Dietrich
Keyword(s):  
Calcium Oxalate ◽  
Aluminium Hydroxide ◽  
Barium Sulfate ◽  
Anticoagulant Effect ◽  
Normal Plasma ◽  
Oxalate Ion

SummaryHeparinized blood or plasma coagulates if, after addition of oxalate, recalcification follows. Of the decalcifying agents only oxalate ion has been suitable for demonstrating this phenomenon. Oxalate seem to accomplish two different roles connected with this effect: a fundamental one, i. e., to sensitize a heparinlipoprotein complex to the action of an anti-heparin factor found in normal plasma or serum and a secondary one, related to its capacity to adsorb this antiheparin factor. The latter is removable by centrifugation. This anti-heparin oxalate factor, which is able to counteract the action of heparin after previous addition of oxalate, was found in sequestrened, Dowex 50 resin plasma or in serum, but is not active in citrated plasma. This factor was removed from plasma by adsorption with barium sulfate, aluminium hydroxide or calcium oxalate and was eluted from these adsorbants after incubation with saline.

A Simple Method for Preparing Fibrinogen

1966 ◽  
Vol 16 (01/02) ◽  
pp. 198-206 ◽  
Author(s):  
W Straughn ◽  
R. H Wagner
Keyword(s):  
Barium Sulfate ◽  
Caproic Acid ◽  
Aminobutyric Acid ◽  
Gamma Aminobutyric Acid ◽  
Human Fibrinogen ◽  
Simple Method ◽  
High Yields ◽  
Marked Stability

SummaryA simple new procedure is reported for the isolation of canine, bovine, porcine, and human fibrinogen. Two molar β-alanine is used to precipitate fibrinogen from barium sulfate adsorbed plasma. The procedure is characterized by dependability and high yields. The material is 95% to 98% clottable protein but still contains impurities such as plasminogen and fibrin-stabilizing factor. Plasminogen may be removed by adsorption with charcoal. The fibrinogen preparations exhibit marked stability to freezing, lyophilization, and dialysis. Epsilon-amino-n-caproic acid and gamma-aminobutyric acid which were also studied have the property of precipitating proteins from plasma but lack the specificity for fibrinogen found with β-alanine.

Oxidation Companied by Scale Removal: Initial and Asymptotical Kinetics

2008 ◽  
Vol 45 (7) ◽  
pp. 662-667 ◽  
Author(s):  
Yitung CHEN ◽  
Taide TAN ◽  
Huajun CHEN
Keyword(s):  
Scale Removal

scholarly journals Crystallization Behavior and Mechanical Properties of Poly(ε-caprolactone) Reinforced with Barium Sulfate Submicron Particles

Materials ◽  
2021 ◽  
Vol 14 (9) ◽  
pp. 2368
Author(s):  
Hegoi Amestoy ◽  
Paul Diego ◽  
Emilio Meaurio ◽  
Jone Muñoz ◽  
Jose-Ramon Sarasua
Keyword(s):  
Barium Sulfate ◽  
Thermal Studies ◽  
Polarized Light ◽  
Optical Microscope ◽  
Submicron Particles ◽  
Degree Of Crystallinity ◽  
Scanning Calorimetry ◽  
Nucleation Effect ◽  
Crystal Fraction ◽  
Light Optical Microscope

Poly(ε-caprolactone) (PCL) was mixed with submicron particles of barium sulfate to obtain biodegradable radiopaque composites. X-ray images comparing with aluminum samples show that 15 wt.% barium sulfate (BaSO4) is sufficient to present radiopacity. Thermal studies by differential scanning calorimetry (DSC) show a statistically significant increase in PCL degree of crystallinity from 46% to 52% for 25 wt.% BaSO4. Non-isothermal crystallization tests were performed at different cooling rates to evaluate crystallization kinetics. The nucleation effect of BaSO4 was found to change the morphology and quantity of the primary crystals of PCL, which was also corroborated by the use of a polarized light optical microscope (PLOM). These results fit well with Avrami–Ozawa–Jeziorny model and show a secondary crystallization that contributes to an increase in crystal fraction with internal structure reorganization. The addition of barium sulfate particles in composite formulations with PCL improves stiffness but not strength for all compositions due to possible cavitation effects induced by debonding of reinforcement interphase.

scholarly journals A scale removal and scale absorption method for circulating water system

2021 ◽  
Vol 676 (1) ◽  
pp. 012099
Author(s):  
Yao Yang ◽  
Xiaona Li ◽  
Xiang Li ◽  
Yuchao Li ◽  
Tianqi Meng ◽  
...  
Keyword(s):  
Water System ◽  
Absorption Method ◽  
Scale Removal ◽  
Circulating Water ◽  
Circulating Water System

Suppressing Barium Sulfate Crystallization with Hydroxycitrate: A Dual Nucleation and Growth Inhibitor

2021 ◽  
Author(s):  
Ricardo D. Sosa ◽  
Xi Geng ◽  
Jacinta C. Conrad ◽  
Michael A. Reynolds ◽  
Jeffrey D. Rimer
Keyword(s):  
Barium Sulfate ◽  
Growth Inhibitor ◽  
Nucleation And Growth

scholarly journals Enzyme-catalyzed biodegradation of penicillin fermentation residues by β-lactamase OtLac from Ochrobactrum tritici

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Peng Wang ◽  
Chen Shen ◽  
Qinqin Cong ◽  
Kaili Xu ◽  
Jialin Lu
Keyword(s):  
Large Scale ◽  
In Vitro Study ◽  
Scale Removal ◽  
E Coli ◽  
Penicillin V ◽  
Highly Active ◽  
Steady State Kinetics ◽  
Biodegradation Process ◽  
Km Value

Abstract Background Biodegradation of antibiotics is a promising method for the large-scale removal of antibiotic residues in the environment. However, the enzyme that is involved in the biodegradation process is the key information to be revealed. Results In this study, the beta-lactamase from Ochrobactrumtritici that mediates the biodegradation of penicillin V was identified and characterized. When searching the proteins of Ochrobactrumtritici, the β-lactamase (OtLac) was identified. OtLac consists of 347 amino acids, and predicted isoelectric point is 7.0. It is a class C β-lactamase according to BLAST analysis. The coding gene of OtLac was amplified from the genomic DNA of Ochrobactrumtritici. The OtLac was overexpressed in E. coli BL21 (DE3) and purified with Ni2+ column affinity chromatography. The biodegradation ability of penicillin V by OtLac was identified in an in vitro study and analyzed by HPLC. The optimal temperature for OtLac is 32 ℃ and the optimal pH is 7.0. Steady-state kinetics showed that OtLac was highly active against penicillin V with a Km value of 17.86 μM and a kcat value of 25.28 s−1 respectively. Conclusions OtLac demonstrated biodegradation activity towards penicillin V potassium, indicating that OtLac is expected to degrade penicillin V in the future.

Sign in / Sign up

Export Citation Format

Share Document