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Related Concept Videos

Titration Calculations: Weak Acid - Strong Base03:55

Titration Calculations: Weak Acid - Strong Base

49.3K
Calculating pH for Titration Solutions: Weak Acid/Strong Base
For the titration of 25.00 mL of 0.100 M CH3CO2H with 0.100 M NaOH, the reaction can be represented as:
49.3K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

15.1K
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
15.1K
Titration Calculations: Strong Acid - Strong Base02:28

Titration Calculations: Strong Acid - Strong Base

34.0K
Calculating pH for Titration Solutions: Strong Acid/Strong Base
A titration is carried out for 25.00 mL of 0.100 M HCl (strong acid) with 0.100 M of a strong base NaOH. The pH at different volumes of added base solution can be calculated as follows:
(a) Titrant volume = 0 mL. The solution pH is due to the acid ionization of HCl. Because this is a strong acid, the ionization is complete and the hydronium ion molarity is 0.100 M. The pH of the solution is then:
34.0K
Calculating pH Changes in a Buffer Solution02:45

Calculating pH Changes in a Buffer Solution

58.7K
A buffer can prevent a sudden drop or increase in the pH of a solution after the addition of a strong acid or base up to its buffering capacity; however, such addition of a strong acid or base does result in the slight pH change of the solution. The small pH change can be calculated by determining the resulting change in the concentration of buffer components, i.e., a weak acid and its conjugate base or vice versa. The concentrations obtained using these stoichiometric calculations can be used...
58.7K
Calculating Standard Free Energy Changes02:49

Calculating Standard Free Energy Changes

25.4K
The free energy change for a reaction that occurs under the standard conditions of 1 bar pressure and at 298 K is called the standard free energy change. Since free energy is a state function, its value depends only on the conditions of the initial and final states of the system. A convenient and common approach to the calculation of free energy changes for physical and chemical reactions is by use of widely available compilations of standard state thermodynamic data. One method involves the...
25.4K
Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

654
Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
654

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A Whole Body Dosimetry Protocol for Peptide-Receptor Radionuclide Therapy PRRT: 2D Planar Image and Hybrid 2D+3D SPECT/CT Image Methods
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Count-based method for specific binding ratio calculation in [I-123]FP-CIT SPECT analysis.

Mahmudur G M Rahman1, Muhammad M Islam1,2, Tetsuya Tsujikawa1

  • 1Biomedical Imaging Research Center, University of Fukui, 23-3, Matsuoka-Shimaizuki, Eiheiji, Fukui, 910-1193, Japan.

Annals of Nuclear Medicine
|October 3, 2018
PubMed
Summary
This summary is machine-generated.

A new method for calculating specific binding ratio (SBR) in dopamine transporter (DAT) imaging offers improved reproducibility and diagnostic accuracy for parkinsonian syndromes (PS) and dementia with Lewy body (DLB). This technique enhances clinical diagnosis and disease severity assessment in follow-up studies.

Keywords:
ACSCCTACDATSBR[I-123]ioflupane (FP-CIT) SPECT

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Area of Science:

  • Nuclear medicine imaging
  • Neuroscience
  • Radiochemistry

Background:

  • Dopamine transporter (DAT) imaging is crucial for diagnosing parkinsonian syndromes (PS) and dementia with Lewy body (DLB).
  • Accurate calculation of specific binding ratio (SBR) is essential for reliable DAT imaging interpretation.
  • Existing methods for SBR calculation may have limitations in reproducibility and precision.

Purpose of the Study:

  • To develop and validate a novel method for extracting the striatal volume of interest (VOI) for SBR calculation in [123I]ioflupane (FP-CIT) SPECT.
  • To assess the reproducibility and diagnostic accuracy of the new SBR calculation method compared to a standard method.

Main Methods:

  • A cohort of 200 patients with suspected PS or DLB underwent FP-CIT SPECT imaging.
  • A new method for striatal VOI extraction based on high counts and average striatal volume was developed.
  • SBR was calculated using the new method and compared with the Tossici-Bolt method (SBRBolt), with reproducibility assessed by two operators.

Main Results:

  • The proposed method demonstrated significantly lower coefficients of variation for SBR compared to SBRBolt (p < 0.001), indicating improved reproducibility.
  • No significant differences in SBR were observed between the two operators using the new method.
  • The diagnostic accuracies for PS and DLB using the new method were high, at 98.4% and 96.0%, respectively.

Conclusions:

  • The novel SBR calculation method for FP-CIT SPECT offers enhanced reproducibility and high diagnostic accuracy.
  • This method is valuable for clinical diagnosis of PS and DLB.
  • The improved SBR calculation can aid in assessing disease severity during follow-up studies.