scholarly journals Quantitative LC–MS/MS analysis of arachidonoyl amino acids in mouse brain with treatment of FAAH inhibitor

2013 ◽  
Vol 432 (2) ◽  
pp. 74-81 ◽  
Author(s):  
Bingnan Han ◽  
Rachel Wright ◽  
Aaron M. Kirchhoff ◽  
Julia A. Chester ◽  
Bruce R. Cooper ◽  
...  
Keyword(s):  
Amino Acids ◽  
Mouse Brain ◽  
Ms Analysis

scholarly journals A VIRUS EFFECT ON THE UPTAKE OF C14 FROM GLUCOSE IN VITRO BY AMINO ACIDS IN MOUSE BRAIN

1951 ◽  
Vol 193 (1) ◽  
pp. 205-217
Author(s):  
MaxE. Rafelson ◽  
RichardJ. Winzler ◽  
HaroldE. Pearson
Keyword(s):  
Amino Acids ◽  
Mouse Brain

Comparison of silylation and esterification/acylation procedures in GC-MS analysis of amino acids

2003 ◽  
Vol 26 (17) ◽  
pp. 1474-1478 ◽  
Author(s):  
Tim G. Sobolevsky ◽  
Alexander I. Revelsky ◽  
Barbara Miller ◽  
Vincent Oriedo ◽  
Elena S. Chernetsova ◽  
...  
Keyword(s):  
Amino Acids ◽  
Ms Analysis

scholarly journals Quantification of amino acids and peptides in an ionic liquid based aqueous two-phase system by LC–MS analysis

AMB Express ◽  
2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Sebastian Oppermann ◽  
Christina Oppermann ◽  
Miriam Böhm ◽  
Toni Kühl ◽  
Diana Imhof ◽  
...  
Keyword(s):  
Amino Acids ◽  
Ionic Liquid ◽  
Phase System ◽  
Two Phase ◽  
Aqueous Two Phase System ◽  
Ms Analysis

Untersuchungen zur Struktur und Derivatisierung von Kondensationsprodukten der 2,4-Diaminobuttersäure mit anderen Aminosäuren / Investigations Regarding Structure and Derivatization of the Condensation Products of 2,4-Diaminobutyric Acid with Other Amino Acids

1994 ◽  
Vol 49 (1-2) ◽  
pp. 18-25 ◽  
Author(s):  
G. Filsak ◽  
K. Taraz ◽  
H. Budzikiewicz
Keyword(s):  
Amino Acids ◽  
Fluorescent Pseudomonads ◽  
Peptide Chain ◽  
Diaminobutyric Acid ◽  
Condensation Products ◽  
Ms Analysis ◽  
Model Substances

Condensation of 2,4-diaminobutyric acid (Dab) with other amino acids yields tetrahydropyrimidine derivatives. Such condensation products can be constituents of the peptide chain of pyoverdins and ferribactins (the siderophors of fluorescent pseudomonads). Synthesis of several representatives and model substances allows to confirm earlier structural conclusions based mainly on NMR evidence. Apparent anomalies accompanying the derivatization for GC/MS analysis could be clarified.

Sample collection and amino acids analysis of extracellular fluid of mouse brain slices with low flow push–pull perfusion

The Analyst ◽  
2015 ◽  
Vol 140 (19) ◽  
pp. 6563-6570 ◽  
Author(s):  
G. Ojeda-Torres ◽  
L. Williams ◽  
D. E. Featherstone ◽  
S. A. Shippy
Keyword(s):  
Amino Acids ◽  
Brain Tissue ◽  
Mouse Brain ◽  
Brain Slices ◽  
Extracellular Fluid ◽  
Low Flow ◽  
Sample Collection ◽  
Tissue Slices ◽  
Extracellular Glutamate

Low flow push–pull perfusion is used to measure extracellular glutamate levels from mouse brain tissue slices.

scholarly journals Cloning of cDNAs encoding two related 100-kD coated vesicle proteins (alpha-adaptins).

1989 ◽  
Vol 108 (3) ◽  
pp. 833-842 ◽  
Author(s):  
M S Robinson
Keyword(s):  
Amino Acids ◽  
Mouse Brain ◽  
Southern Blotting ◽  
Protein Sequences ◽  
Coated Vesicles ◽  
Coated Vesicle ◽  
Coat Proteins ◽  
Cell Type ◽  
Brain Cdna Library

Coat proteins of approximately 100-kD (adaptins) are components of the adaptor complexes which link clathrin to receptors in coated vesicles. The alpha-adaptins, which are found exclusively in endocytic coated vesicles, separate into two bands on SDS gels, designated A and C (Robinson, M. S., 1987. J. Cell Biol. 104:887-895). Two distinct cDNAs (sequences 1 and 2) encoding the two alpha-adaptins were cloned from a mouse brain cDNA library. Southern blotting indicates that there is one copy of each of the two alpha-adaptin genes, and that there are no additional closely related genes. Based on the size of the predicted protein products of the two genes (108 and 104 kD), the relative abundance of the two messages in brain and liver, and the reactivity of a sequence 1 fusion protein with different antibodies, it was possible to conclude that sequence 1 codes for A and sequence 2 for C. The two protein sequences are strikingly homologous to each other (84% identical amino acids), the major difference being an additional stretch of 41 amino acids, rich in prolines and acidic residues, inserted into the COOH-terminal half of A. In situ hybridization carried out on mouse brain sections indicates that the same cell type may express both transcripts, but that their relative expressions vary. Antipeptide antibodies are now being raised to find out whether the proteins are localized in functionally distinct populations of endocytic coated vesicles.

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