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Merck

T9878

Sigma-Aldrich

Tyr-Leu

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About This Item

Fórmula empírica (notación de Hill):
C15H22N2O4
Número de CAS:
Peso molecular:
294.35
MDL number:
UNSPSC Code:
12352200
PubChem Substance ID:

storage temp.

−20°C

SMILES string

CC(C)CC(NC(=O)C(N)Cc1ccc(O)cc1)C(O)=O

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Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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M M Mullally et al.
Biological chemistry Hoppe-Seyler, 377(4), 259-260 (1996-04-01)
Novel angiotensin-I-converting enzyme (ACE) inhibitory activities were detected in synthetic peptides corresponding to sequences of beta-lactoglobulin and alpha-lactalbumin and which are known to possess opioid activity. Using hippuryl-histidyl-leucine as substrate, the tetrapeptides beta-lactorphin (Tyr-Leu-Leu-Phe), alpha-lactorphin (Tyr-Gly-Leu-Phe) and beta-lactotensin (His-Ile-Arg-Leu) were
Norimasa Kanegawa et al.
FEBS letters, 584(3), 599-604 (2009-12-17)
We found that Tyr-Leu (YL) dose-dependently exhibits potent anxiolytic-like activity (0.1-1mg/kg, i.p.) comparable to diazepam in the elevated plus-maze test in mice. YL was orally active (0.3-3mg/kg). A retro-sequence peptide or a mixture of Tyr and Leu was inactive. The
Takafumi Mizushige et al.
Neuroscience letters, 543, 126-129 (2013-04-11)
We previously reported that Tyr-Leu (YL) exhibits potent anxiolytic-like activity comparable to diazepam in mice. In the current study, we revealed that aromatic amino acid-Leu, Phe-Leu and Trp-Leu (FL and WL, respectively), exhibited anxiolytic-like activity in the elevated plus-maze and
Ying Chen et al.
The Analyst, 136(9), 1852-1858 (2011-03-12)
In this paper, we developed a simple and effective on-line focusing technique combining dynamic pH junction and sweeping by capillary electrophoresis (CE) with laser-induced fluorescence (LIF) detection. Dynamic pH junction-sweeping is defined when the sample has a different buffer pH
Conceição Fonseca et al.
Journal of mass spectrometry : JMS, 44(5), 681-693 (2009-01-07)
The exposure of peptides and proteins to reactive hydroxyl radicals results in covalent modifications of amino acid side-chains and protein backbone. In this study we have investigated the oxidation the isomeric peptides tyrosine-leucine (YL) and leucine-tyrosine (LY), by the hydroxyl

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