Postnatal development and kinetics of [3H]gaboxadol binding in rat brain: In vitro homogenate binding and quantitative autoradiography

2007 ◽  
Vol 1170 ◽  
pp. 39-47 ◽  
Author(s):  
Anne Friemel ◽  
Bjarke Ebert ◽  
Pete H. Hutson ◽  
Peter Brust ◽  
Karen Nieber ◽  
...  
Keyword(s):  
Rat Brain ◽  
Postnatal Development ◽  
Quantitative Autoradiography ◽  
Kinetics Of

The in vitro dissociation kinetics of (R,R)-[125I]4IQNB is reflected in the in vivo washout of the radioligand from rat brain

Life Sciences ◽  
1992 ◽  
Vol 50 (9) ◽  
pp. 629-637 ◽  
Author(s):  
Raymond E. Gibson ◽  
Terry Moody ◽  
Timothy A. Schneidau ◽  
Elaine M. Jagoda ◽  
Richard C. Reba
Keyword(s):  
Rat Brain ◽  
Dissociation Kinetics ◽  
Kinetics Of

Some properties of aminopeptidase associated with rat brain cortical synaptosomes

1983 ◽  
Vol 61 (11) ◽  
pp. 1185-1190 ◽  
Author(s):  
William W.-C. Chan ◽  
Wolfgang Demmer ◽  
Karl Brand
Keyword(s):  
Rat Brain ◽  
Leucine Aminopeptidase ◽  
Single Species ◽  
Bound State ◽  
Spectrophotometric Assay ◽  
Diethyl Pyrocarbonate ◽  
Kinetics Of ◽  
The Brain

To understand the breakdown of peptides in the brain, we studied the aminopeptidase associated with synaptosome particles. A continuous spectrophotometric assay in stirred cuvettes was used to follow the kinetics of inactivation by EDTA and by diethyl pyrocarbonate. The sensitivity of the enzyme towards puromycin and leucine hydroxamate was also determined. The results are consistent with the presence of a single species of aminopeptidase in freshly prepared synaptosome. This enzyme is capable of degrading Met-enkephalin in vitro and is distinct from microsomal leucine aminopeptidase. Storage of synaptosomes by freezing and subsequent thawing changed some properties of the enzyme and partially solubilized the enzyme. These studies suggest that there are advantages in studying the enzyme in its native particle-bound state.

Effect of pH and inhibitors on beta-amyloid fibril assembly

1996 ◽  
Vol 54 ◽  
pp. 752-753
Author(s):  
Beverly E. Maleeff ◽  
Timothy K. Hart ◽  
Stephen J. Wood ◽  
Ronald Wetzel
Keyword(s):  
Amyloid Fibril ◽  
Peptide Fragment ◽  
Hydrophobic Peptides ◽  
Amyloid Fibril Formation ◽  
Effects Of Ph ◽  
Severity Of The Disease ◽  
Kinetics Of ◽  
The Brain

Alzheimer's disease is characterized post-mortem in part by abnormal extracellular neuritic plaques found in brain tissue. There appears to be a correlation between the severity of Alzheimer's dementia in vivo and the number of plaques found in particular areas of the brain. These plaques are known to be the deposition sites of fibrils of the protein β-amyloid. It is thought that if the assembly of these plaques could be inhibited, the severity of the disease would be decreased. The peptide fragment Aβ, a precursor of the p-amyloid protein, has a 40 amino acid sequence, and has been shown to be toxic to neuronal cells in culture after an aging process of several days. This toxicity corresponds to the kinetics of in vitro amyloid fibril formation. In this study, we report the biochemical and ultrastructural effects of pH and the inhibitory agent hexadecyl-N-methylpiperidinium (HMP) bromide, one of a class of ionic micellar detergents known to be capable of solubilizing hydrophobic peptides, on the in vitro assembly of the peptide fragment Aβ.

Kinetics of Various 99mTc-Sn-Pyrophosphate Compounds in the Rat

1977 ◽  
Vol 16 (04) ◽  
pp. 157-162 ◽  
Author(s):  
C. Schümichen ◽  
B. Mackenbrock ◽  
G. Hoffmann
Keyword(s):  
Normal Saline ◽  
Half Life ◽  
Compound A ◽  
Short Half Life ◽  
Low Concentrations ◽  
The Stability ◽  
Kinetics Of ◽  
In Vitro Stability

SummaryThe bone-seeking 99mTc-Sn-pyrophosphate compound (compound A) was diluted both in vitro and in vivo and proved to be unstable both in vitro and in vivo. However, stability was much better in vivo than in vitro and thus the in vitro stability of compound A after dilution in various mediums could be followed up by a consecutive evaluation of the in vivo distribution in the rat. After dilution in neutral normal saline compound A is metastable and after a short half-life it is transformed into the other 99mTc-Sn-pyrophosphate compound A is metastable and after a short half-life in bone but in the kidneys. After dilution in normal saline of low pH and in buffering solutions the stability of compound A is increased. In human plasma compound A is relatively stable but not in plasma water. When compound B is formed in a buffering solution, uptake in the kidneys and excretion in urine is lowered and blood concentration increased.It is assumed that the association of protons to compound A will increase its stability at low concentrations while that to compound B will lead to a strong protein bond in plasma. It is concluded that compound A will not be stable in vivo because of a lack of stability in the extravascular space, and that the protein bond in plasma will be a measure of its in vivo stability.

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