Comparative Analysis of Three-Versus Two-dimensional Imaging in Laparoscopic Cholecystectomy

2021 ◽  
Author(s):  
Asta Tauriainen ◽  
Fausto Biancari ◽  
Tuomas Tauriainen
Keyword(s):  
Laparoscopic Cholecystectomy ◽  
Comparative Analysis ◽  
Two Dimensional

Investigation of two-dimensional nonstationary processes of outflow a gas-saturated liquid from axisymmetric vessels

2012 ◽  
Vol 9 (1) ◽  
pp. 47-52
Author(s):  
R.Kh. Bolotnova ◽  
V.A. Buzina
Keyword(s):  
Comparative Analysis ◽  
Numerical Model ◽  
Liquid Mixture ◽  
Phase Model ◽  
Test Problems ◽  
Two Dimensional ◽  
Nonstationary Processes ◽  
Saturated Liquid ◽  
Two Phase ◽  
One Dimensional

The two-dimensional and two-phase model of the gas-liquid mixture is constructed. The validity of numerical model realization is justified by using a comparative analysis of test problems solution with one-dimensional calculations. The regularities of gas-saturated liquid outflow from axisymmetric vessels for different geometries are established.

Comparative analysis of robotic-assisted versus laparoscopic cholecystectomy in pediatric patients

2020 ◽  
Author(s):  
Afif N. Kulaylat ◽  
Holden Richards ◽  
Keigo Yada ◽  
David Coyle ◽  
Rita Shelby ◽  
...  
Keyword(s):  
Laparoscopic Cholecystectomy ◽  
Comparative Analysis ◽  
Pediatric Patients ◽  
Robotic Assisted

scholarly journals Biochemical analysis of actin in crane-fly gonial cells: evidence for actin in spermatocytes and spermatids--but not sperm.

1980 ◽  
Vol 86 (1) ◽  
pp. 315-325 ◽  
Author(s):  
A R Strauch ◽  
E J Luna ◽  
J R LaFountain
Keyword(s):  
Molecular Weight ◽  
Comparative Analysis ◽  
Gel Electrophoresis ◽  
Biochemical Analysis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Cell Types ◽  
Two Dimensional ◽  
Peptide Analysis ◽  
General Applicability ◽  
Peptide Maps

A biochemical assay employing DNase-I affinity chromatography, two-dimensional peptide analysis and SDS polyacrylamide gel electrophoresis was used to isolate, identify, and assess the amount of actin from gonial cells of the crane fly, Nephrotoma suturalis. Based on the analysis of cell homogenates under conditions in which all cellular actin is converted to the monomeric DNase-binding form, actin comprises approximately 1% of the total protein in homogenates of spermatocytes and spermatids. SDS gel analysis of mature sperm reveals no polypeptides with a molecular weight similar to that of actin. Under conditions that preserve native supramolecular states of actin, approximately 80% of the spermatocyte actin is in a sedimentable form whereas only approximately 30% of the spermatid actin is sedimentable. These differences could be meaningful with regard to strutural changes that occur during spermiogenesis. A comparative analysis of two-dimensional peptide maps of several radioiodinated actins reveals similarities among spermatocyte, spermatid, and human erythrocyte actins. The results suggest the general applicability of this approach to other cell types that contain limited amounts of actin.

scholarly journals Comparative analysis by two-dimensional iodopeptide mapping of the RhD protein and LW glycoprotein

Blood ◽  
1990 ◽  
Vol 75 (11) ◽  
pp. 2245-2249 ◽  
Author(s):  
C Bloy ◽  
P Hermand ◽  
B Cherif-Zahar ◽  
HH Sonneborn ◽  
JP Cartron
Keyword(s):  
Monoclonal Antibodies ◽  
Comparative Analysis ◽  
Primary Amine ◽  
Protein Domains ◽  
Two Dimensional ◽  
Tyrosine Residues ◽  
Chloramine T ◽  
Carbohydrate Chains

Abstract The RhD polypeptide and LW glycoprotein were separately immunopurified with monoclonal antibodies and compared by two-dimensional (2-D) iodopeptide mapping after digestion with alpha-chymotrypsin. These proteins have distinct 2-D maps, as seen after 125I-labeling tyrosine residues (chloramine-T procedure), and even more strikingly after labeling primary amine residues (Bolton-Hunter procedure). Of the more than 20 iodopeptides visualized, only five migrated identically when preparations of RhD and LW were directly compared, suggesting that RhD and LW are different proteins that may share some common protein domains. N-glycanase treatment of the iodopeptides did not modify the 2- D map of the RhD protein but greatly affected the LW map, further indicating that LW, but not RhD, carries N-linked carbohydrate chains. After deglycosylation the LW map was different from the RhD map, confirming that the RhD and LW polypeptides are different proteins. These findings demonstrate that LW is neither a glycosylated form of Rh protein nor is Rh a precursor of LW.

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