scholarly journals Subxiphoid uniportal bilateral lung wedge resection

2020 ◽  
Vol 58 (Supplement_1) ◽  
pp. i100-i102
Author(s):  
Takahiro Negi ◽  
Takashi Suda ◽  
Sachiko Tochii ◽  
Yasushi Hoshikawa
Keyword(s):  
Wedge Resection ◽  
Lung Resection ◽  
Detailed Comparison ◽  
Intercostal Nerve ◽  
Xiphoid Process ◽  
One Stage ◽  
Bilateral Surgery ◽  
Bilateral Lung ◽  
The One ◽  
Initial Results

Abstract Subxiphoid uniportal bilateral lung wedge resection, in which all manipulations are performed via a 3-cm wound positioned below the xiphoid process, can be performed in the supine position without the patient having to change positions. It also enables one-stage bilateral lung resection. We report the surgical procedure and initial results of subxiphoid uniportal bilateral lung wedge resection. A 3-cm transverse incision was made 1 cm caudally below the xiphoid process. A port for uniportal surgery was inserted. After CO2 insufflation at 8 mmHg, the lung was grasped and lifted with bent grasping forceps, and by bending the tip of a stapler, the surgeon resected the affected portion of the bilateral lungs. In this approach, there is one incision, no intercostal nerve damage and bilateral surgery can be performed in the same procedure; therefore, the technique may have the benefit of lesser invasiveness for the patient. Furthermore, a detailed comparison of subxiphoid uniportal bilateral lung wedge resection with the one-stage lateral intercostal approach with a larger subject sample is needed.

Performances of an Artificial Reagent for the One-stage Factor IX Assay

1975 ◽  
Vol 33 (03) ◽  
pp. 547-552 ◽  
Author(s):  
L Meunier ◽  
J. P Allain ◽  
D Frommel
Keyword(s):  
Human Plasma ◽  
Factor Ix ◽  
Severe Haemophilia ◽  
Normal Human Plasma ◽  
Haemophilia B ◽  
One Stage ◽  
Normal Human ◽  
The One

SummaryA mixture of adsorbed normal human plasma and chicken plasma was prepared as reagent for factor IX measurement using a one-stage method. The substrate was found to be specific for factor IX. Its performances tested on samples displaying factor IX activity ranging from <l%–2,500% compared favorably with those obtained when using the plasma of severe haemophilia B patients as substrate.

The Effects of Amines on the Esterase Activities of Thrombin and Thrombokinase and on Several Clotting Tests

1974 ◽  
Vol 31 (02) ◽  
pp. 309-318
Author(s):  
Phyllis S Roberts ◽  
Raphael M Ottenbrite ◽  
Patricia B Fleming ◽  
James Wigand
Keyword(s):  
Choline Chloride ◽  
Polymerization Process ◽  
Ammonium Bromide ◽  
Bovine Thrombin ◽  
One Stage ◽  
Human Proteins ◽  
Rate Of Hydrolysis ◽  
The One ◽  
Hydrolysis Of Esters ◽  
Hydrolysis Of

Summary1. Choline chloride, 0.1 M (in 0.25 M Tris. HCl buffer, pH 7.4 or 8.0, 37°), doubles the rate of hydrolysis of TAME by bovine thrombokinase but has no effect on the hydrolysis of this ester by either human or bovine thrombin. Only when 1.0 M or more choline chloride is present is the hydrolysis of BAME by thrombokinase or thrombin weakly inhibited. Evidence is presented that shows that these effects are due to the quaternary amine group.2. Tetramethyl ammonium bromide or chloride has about the same effects on the hydrolysis of esters by these enzymes as does choline chloride but tetra-ethyl, -n.propyl and -n.butyl ammonium bromides (0.1 M) are stronger accelerators of the thrombokinase-TAME reaction and they also accelerate, but to a lesser degree, the thrombin-TAME reaction. In addition, they inhibit the hydrolysis of BAME by both enzymes. Their effects on these reactions, however, do not follow any regular order. The tetraethyl compound is the strongest accelerator of the thrombokinase-TAME reaction but the tetra-ethyl and -butyl compounds are the strongest accelerators of the thrombin-TAME reaction. The ethyl and propyl compounds are the best (although weak) inhibitors of the thrombokinase-BAME and the propyl compound of the thrombin-BAME reactions.3. Tetra-methyl, -ethyl, -n.propyl and -n.butyl ammonium bromides (0.01 M) inhibit the clotting of fibrinogen by thrombin (bovine and human proteins) at pH 7.4, imidazole or pH 6.1, phosphate buffers and they also inhibit, but to a lesser degree, a modified one-stage prothrombin test. In all cases the inhibition increases regularly as the size of the alkyl group increases from methyl to butyl. Only the ethyl com pound (0.025 M but not 0.01 M), however, significantly inhibits the polymerization of bovine fibrin monomers. It was concluded that inhibition of the fibrinogen-thrombin and the one-stage tests by the quaternary amines is not due to any effect of the com pounds on the polymerization process but probably due to inhibition of thrombin’s action on fibrinogen by the quaternary amines.

The Formation of Intermediate Product I in a Purified System The Role of Factor IX or of its Precursor and of a Hageman Factor-PTA Fraction

1961 ◽  
Vol 6 (02) ◽  
pp. 224-234 ◽  
Author(s):  
E. T Yin ◽  
F Duckert
Keyword(s):  
Intermediate Product ◽  
Factor Ix ◽  
Assay Method ◽  
Lag Phase ◽  
Factor X ◽  
Haemophilia B ◽  
Hageman Factor ◽  
One Stage ◽  
The One

Summary1. The role of two clot promoting fractions isolated from either plasma or serum is studied in a purified system for the generation of intermediate product I in which the serum is replaced by factor X and the investigated fractions.2. Optimal generation of intermediate product I is possible in the purified system utilizing fractions devoid of factor IX one-stage activity. Prothrombin and thrombin are not necessary in this system.3. The fraction containing factor IX or its precursor, no measurable activity by the one-stage assay method, controls the yield of intermediate product I. No similar fraction can be isolated from haemophilia B plasma or serum.4. The Hageman factor — PTA fraction shortens the lag phase of intermediate product I formation and has no influence on the yield. This fraction can also be prepared from haemophilia B plasma or serum.

The Preparation of an Artificial Reagent for the One-Stage Factor VIII Assay

1970 ◽  
Vol 23 (02) ◽  
pp. 306-312 ◽  
Author(s):  
D Nyman
Keyword(s):  
Factor Viii ◽  
Artificial Substrate ◽  
One Stage ◽  
The One

SummaryA method for preparation of an artificial substrate for the one-stage factor VIII assay is described. Standardization of the test is given. The method is specific and reproducible.

The Reaction of Thiol Compounds with the Vitamin-K Dependent Clotting Factors

1969 ◽  
Vol 21 (03) ◽  
pp. 573-579 ◽  
Author(s):  
P Fantl
Keyword(s):  
Prothrombin Time ◽  
Vitamin K ◽  
Anaerobic Conditions ◽  
Clotting Factors ◽  
Thiol Compounds ◽  
Aerobic Conditions ◽  
One Stage ◽  
Factor Ii ◽  
Ph Dependent ◽  
The One

SummaryTreatment of human and dog oxalated plasma with 0.2 to 1.0 × 10−1 M 2.3-dithiopropanol (BAL) or dithiothreitol (DTT) at 2–4° C for 30 min results in the reduction of the vitamin-K dependent clotting factors II, VII, IX and X to the respective-SH derivatives. The reaction is pH dependent. Under aerobic conditions the delayed one stage prothrombin time can be partly reversed. Under anaerobic conditions a gradual prolongation of the one stage prothrombin time occurs without reversal.In very diluted plasma treated with the dithiols, prothrombin can be converted into thrombin if serum as source of active factors VII and X is added. In contrast SH factors VII, IX and X are inactive in the specific tests. Reoxidation to active factors II, VII, IX and X takes place during adsorption and elution of the SH derivatives. The experiments have indicated that not only factor II but also factors VII, IX and X have active-S-S-centres.

Two-Stage Procedure for the Quantitative Determination of Autoprothrombin III Concentration and Some Applications

1967 ◽  
Vol 18 (01/02) ◽  
pp. 198-210 ◽  
Author(s):  
Ronald S Reno ◽  
Walter H Seegers
Keyword(s):  
Prothrombin Time ◽  
Factor Vii ◽  
Two Stage ◽  
Pronounced Increase ◽  
One Stage ◽  
Assay Procedure ◽  
Bovine Plasma ◽  
The One ◽  
Autoprothrombin C

SummaryA two-stage assay procedure was developed for the determination of the autoprothrombin C titre which can be developed from prothrombin or autoprothrombin III containing solutions. The proenzyme is activated by Russell’s viper venom and the autoprothrombin C activity that appears is measured by its ability to shorten the partial thromboplastin time of bovine plasma.Using the assay, the autoprothrombin C titre was determined in the plasma of several species, as well as the percentage of it remaining in the serum from blood clotted in glass test tubes. Much autoprothrombin III remains in human serum. With sufficient thromboplastin it was completely utilized. Plasma from selected patients with coagulation disorders was assayed and only Stuart plasma was abnormal. In so-called factor VII, IX, and P.T.A. deficiency the autoprothrombin C titre and thrombin titre that could be developed was normal. In one case (prethrombin irregularity) practically no thrombin titre developed but the amount of autoprothrombin C which generated was in the normal range.Dogs were treated with Dicumarol and the autoprothrombin C titre that could be developed from their plasmas decreased until only traces could be detected. This coincided with a lowering of the thrombin titre that could be developed and a prolongation of the one-stage prothrombin time. While the Dicumarol was acting, the dogs were given an infusion of purified bovine prothrombin and the levels of autoprothrombin C, thrombin and one-stage prothrombin time were followed for several hours. The tests became normal immediately after the infusion and then went back to preinfusion levels over a period of 24 hrs.In other dogs the effect of Dicumarol was reversed by giving vitamin K1 intravenously. The effect of the vitamin was noticed as early as 20 min after administration.In response to vitamin K the most pronounced increase was with that portion of the prothrombin molecule which yields thrombin. The proportion of that protein with respect to the precursor of autoprothrombin C increased during the first hour and then started to go down and after 3 hrs was equal to the proportion normally found in plasma.

Standardization of Factor VIII – IV. Establishment of the 3rd International Standard for Factor VIII: C Concentrate

1983 ◽  
Vol 50 (03) ◽  
pp. 697-702 ◽  
Author(s):  
T W Barrowcliffe ◽  
A D Curtis ◽  
D P Thomas
Keyword(s):  
Factor Viii ◽  
High Purity ◽  
Collaborative Study ◽  
World Health ◽  
Current Standard ◽  
Two Stage ◽  
International Standard ◽  
One Stage ◽  
The One ◽  
Health Organization

SummaryAn international collaborative study was carried out to establish a replacement for the current (2nd) international standard for Factor VIII: C, concentrate. Twenty-six laboratories took part, of which 17 performed one-stage assays, three performed two-stage assays and six used both methods. The proposed new standard, an intermediate purity concentrate, was assayed against the current standard, against a high-purity concentrate and against an International Reference Plasma, coded 80/511, previously calibrated against fresh normal plasma.Assays of the proposed new standard against the current standard gave a mean potency of 3.89 iu/ampoule, with good agreement between laboratories and between one-stage and two- stage assays. There was also no difference between assay methods in the comparison of high-purity and intermediate purity concentrates. In the comparison of the proposed standard with the plasma reference preparation, the overall mean potency was 4.03 iu/ampoule, but there were substantial differences between laboratories, and the two-stage method gave significantly higher results than the one stage method. Of the technical variables in the one-stage method, only the activation time with one reagent appeared to have any influence on the results of this comparison of concentrate against plasma.Accelerated degradation studies showed that the proposed standard is very stable. With the agreement of the participants, the material, in ampoules coded 80/556, has been established by the World Health Organization as the 3rd International Standard for Factor VIII :C, Concentrate, with an assigned potency of 3.9 iu/ampoule.

scholarly journals Comparative In Vitro Evaluation of the Primary Stability in D3 Synthetic Bone of Two Different Shapes and Pitches of the Implant Threads

2021 ◽  
Vol 11 (12) ◽  
pp. 5612
Author(s):  
Stefano Fanali ◽  
Margherita Tumedei ◽  
Pamela Pignatelli ◽  
Alessandra Lucchese ◽  
Francesco Inchingolo ◽  
...  
Keyword(s):  
Surgical Techniques ◽  
Primary Stability ◽  
Implant Design ◽  
Insertion Torque ◽  
Synthetic Bone ◽  
One Stage ◽  
Prosthetic Joint ◽  
Joint Connection ◽  
The One

Background: Implant primary stability can be affected by several factors related to implant macrogeometry, local anatomy, and surgical techniques. The aim of this research was to study primary stability on polyurethane foam sheets of wide-threaded implant design compared to narrow-threaded implants. Materials and methods: Two different implant designs were positioned on D3 density polyurethane blocks in a standardized environment: the wide-threaded implant and the narrow-threaded implant, for a total of 160 specimens. Moreover, for each group, two different sizes were considered: 3.8mm × 12mm and 4.8mm × 12 mm. The insertion torque (IT) values, the removal strength (RT), and the Periotest analyses were evaluated. Results: A significantly higher IT and RT was reported for wide-threaded implants and two-stage implants (p < 0.01), compared to the narrow-threaded implants. The diameters seemed to provide a significant effect on the primary stability for both implants’ geometry (p < 0.01). A higher mean of the one-stage implant was evident in the Periotest measurements (p < 0.01). Conclusions: Both of the implants showed sufficient stability in polyurethane artificial simulation, while the wide-threaded implant design showed a higher primary stability on alveolar cancellous synthetic bone in vitro. Additionally, the prosthetic joint connection seemed to have a determinant effect on Periotest analysis, and the one-stage implants seemed to provide a high stability of the fixture when positioned in the osteotomy, which could be important for the immediate loading protocol.

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