scholarly journals Reply to ‘Comment on “Magnitude conversion problem using general orthogonal regression” by H. R. Wason, Ranjit Das and M. L. Sharma’ by Paolo Gasperini and Barbara Lolli

2013 ◽  
Vol 196 (1) ◽  
pp. 628-631 ◽  
Author(s):  
Ranjit Das ◽  
H. R. Wason ◽  
M. L. Sharma
Keyword(s):  
Orthogonal Regression ◽  
Magnitude Conversion

scholarly journals Magnitude conversion problem using general orthogonal regression

2012 ◽  
Vol 190 (2) ◽  
pp. 1091-1096 ◽  
Author(s):  
H. R. Wason ◽  
Ranjit Das ◽  
M. L. Sharma
Keyword(s):  
Orthogonal Regression ◽  
Magnitude Conversion

Effect of Concentration of Trisodium Citrate Anticoagulant on Calculation of the International Normalised Ratio and the International Sensitivity Index of Thromboplastin

1994 ◽  
Vol 72 (01) ◽  
pp. 084-088 ◽  
Author(s):  
E M Duncan ◽  
C R Casey ◽  
B M Duncan ◽  
J V Lloyd
Keyword(s):  
Reference Material ◽  
Oral Anticoagulants ◽  
Reference Method ◽  
Trisodium Citrate ◽  
Sensitivity Index ◽  
Blood Samples ◽  
Orthogonal Regression ◽  
Significant Difference ◽  
International Normalised Ratio ◽  
International Sensitivity Index

SummaryThe aim of this study was to determine whether the concentration of trisodium citrate used to anticoagulate blood has an effect on the INR of the sample and the ISI of the thromboplastin. Five thromboplastins including and Australian reference material were used to measure the prothrombin time of normal and patient samples collected into two concentrations of trisodium citrate - 109 mM and 129 mM. There was no effect of citrate concentration on the INRs determined with the reference material. However for the other four thromboplastins there was a significant difference between INRs for the two citrate groups. The prothrombin times of the samples collected into 129 mM were longer than those collected into 109 mM. This difference was only slight in normal plasma but more marked in patients receiving oral anticoagulants, causing the INRs for patient plasmas collected into 129 mM citrate to be higher then the corresponding samples collected into 109 mM citrate.From orthogonal regression of log prothrombin times by the reference method against each thromboplastin, we found that the ISI for each thromboplastin was approximately 10% lower when determined with samples collected into 129 mM citrate than with samples collected into 109 mM. These results suggest that the concentration of trisodium citrate used for collection of blood samples can affect the calculation of the INR and the calibration of the ISI of thromboplastin. This was found both for commercial thromboplastins prepared by tissue extraction and for a recombinant tissue factor.

Research on Enzymatic Hydrolysis of Whey Protein

2013 ◽  
Vol 411-414 ◽  
pp. 3205-3209
Author(s):  
Fang Qian ◽  
Lei Zhao ◽  
Shu Juan Jiang ◽  
Guang Qing Mu
Keyword(s):  
Enzymatic Hydrolysis ◽  
Whey Protein ◽  
Degree Of Hydrolysis ◽  
Quadratic Regression ◽  
Orthogonal Regression ◽  
Single Factor Analysis ◽  
Verification Test ◽  
Enzyme Dosage ◽  
Hydrolysis Conditions ◽  
Hydrolysis Of

Based on single factor analysis for the enzymatic hydrolysis of whey protein, papain was selected as the optimal enzyme and its enzymatic hydrolysis conditions were optimized by the quadratic regression orthogonal rotary test. The orthogonal regression model for degree of hydrolysis (DH) to three factors including temperature (X1), time (X2), enzyme dosage (X3) was established as follow: DH=10.40+0.22X1+0.30X2+1.31X3+0.019X1X2+0.011X1X3-0.039X2X3-0.39X12-0.16X22-0.40X32, Verification test showed a DH of 11.7% was obtained at the optimal hydrolysis condition of 56.6°C, 113.8 min and enzyme 8213.7 U /g protein, which basically consisted with the model theoretical value.

General Orthogonal Regression Relations between Body-Wave and Moment Magnitudes

2013 ◽  
Vol 84 (2) ◽  
pp. 219-224 ◽  
Author(s):  
R. Das ◽  
H. R. Wason ◽  
M. L. Sharma
Keyword(s):  
Body Wave ◽  
Orthogonal Regression ◽  
Regression Relations

scholarly journals EVOLUTIONARY STRATEGY (μ+λ) AS AN INSTRUMENT FOR DETERMINING DEFORMATION PARAMETERS OF STEEL STRUCTURES

2013 ◽  
Vol 95 (1) ◽  
pp. 23-35 ◽  
Author(s):  
Maria Mrówczyńska
Keyword(s):  
Evolutionary Algorithm ◽  
Global Minimum ◽  
Steel Structures ◽  
Regression Function ◽  
Evolutionary Strategy ◽  
Estimation Of Parameters ◽  
Criterion Function ◽  
Orthogonal Regression ◽  
Deformation Parameters ◽  
Theoretical Analyses

Abstract The article presents the use of an evolutionary algorithm for determining the shape of the guy rope sag of a steel smokestack. The author excludes the analysis of the operation of the rope, and discusses only the problem of determining parameters of the function of the adaption of the rope sag curve into empirical data, obtained by the geodetic method. The estimation of parameters of the curve and the characteristics of the accuracy of its adaption into experimental data were carried out by means of an evolutionary algorithm with the use of an evolutionary strategy (μ+λ). The correctness of the strategy presented in the paper, as an instrument for searching for a global minimum of a criterion function, has been presented using as an example the minimisation of a certain two dimensional function and the estimation of parameters of an ordinary and orthogonal regression function. Previous theoretical analyses have also been used for determining parameters of the guy rope sag of a steel smokestack, which is measured periodically. In addition approximate values of the pull forces in the guy ropes have been calculated.

Vancomycin Serum Protein Binding Determination by Ultrafiltration

1988 ◽  
Vol 22 (4) ◽  
pp. 300-303 ◽  
Author(s):  
Bruce H. Ackerman ◽  
E. Howard Taylor ◽  
Keith M. Olsen ◽  
Wedad Abdel-Malak ◽  
Alexandras A. Pappas
Keyword(s):  
Protein Binding ◽  
Correlation Coefficient ◽  
Pharmacokinetic Study ◽  
Room Temperature ◽  
Total Serum ◽  
Serum Protein Binding ◽  
Serum Concentrations ◽  
Orthogonal Regression ◽  
The Mean ◽  
Serum Vancomycin

Sixty-two serum concentrations were obtained from 12 infected patients enrolled in a vancomycin pharmacokinetic study. Both unbound and total serum vancomycin concentrations were measured using ultrafiltration and a commercial fluorescent polarization immunoassay. Ultrafiltrates were obtained by centrifugation at 1000 × g for ten minutes at room temperature and their assay indicated a range in protein binding from 7.9 to 71 percent. The mean protein binding (mean ±SD) was 41.95 ± 14.15 percent. No measurable adsorption of vancomycin onto the ultrafiltration membrane was noted. Orthogonal regression of unbound versus total vancomycin concentrations was described by the equation y=0.597x-0.362 with a correlation coefficient of 0.948.

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