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L8250

DL-Leucinamide hydrochloride

Name: <SC>DL</SC>-Leucinamide hydrochloride
Brand: SIGMA

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关于此项目

经验公式（希尔记法）:

C₆H₁₄N₂O · HCl

化学文摘社编号:

10466-60-1

分子量:

166.65

UNSPSC Code:

12352200

PubChem Substance ID:

24896497

MDL number:

MFCD00070244

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assay

≥98% (TLC)

form

powder

color

white

SMILES string

Cl.CC(C)CC(N)C(N)=O

InChI

1S/C6H14N2O.ClH/c1-4(2)3-5(7)6(8)9;/h4-5H,3,7H2,1-2H3,(H2,8,9);1H

InChI key

VSPSRRBIXFUMOU-UHFFFAOYSA-N

Biochem/physiol Actions

DL-Leucinamide hydrochloride is a racemic mixture of D- and L- enantiomers of leucinamide. Leucinamide is an amide derivative of leucine found at the C-terminal of various peptides such as the PAR-2 activating peptide SLIGRL-NH(2).

存储类别

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

法规信息

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Molecular mechanism of the inhibitory effect of cobalt ion on thermolysin activity and the suppressive effect of calcium ion on the cobalt ion-dependent inactivation of thermolysin.

Yasuhiko Hashida et al.

Journal of biochemistry, 141(6), 879-888 (2007-04-05)

Thermolysin activity in the hydrolysis of N-[3-(2-furyl)acryloyl]-glycyl-l-leucine amide (FAGLA) and FA-l-leucyl-l-alanine amide (FALAA) was examined at various Co(2+) and Ca(2+) concentrations. It decreased to 28% with increasing [Co(2+)] up to 18 mM. The Co(2+)-dependent inactivation was in part suppressed by

L: -Stereoselective amino acid amidase with broad substrate specificity from Brevundimonas diminuta: characterization of a new member of the leucine aminopeptidase family.

Hidenobu Komeda et al.

Applied microbiology and biotechnology, 70(4), 412-421 (2005-07-08)

Brevundimonas diminuta TPU 5720 produces an amidase acting L-stereoselectively on phenylalaninamide. The enzyme (LaaA(Bd)) was purified to electrophoretic homogeneity by ammonium sulfate fractionation and four steps of column chromatography. The final preparation gave a single band on SDS-PAGE with a

Application of Fourier transform infrared spectroscopy for monitoring hydrolysis and synthesis reactions catalyzed by a recombinant amidase.

R Pacheco et al.

Analytical biochemistry, 346(1), 49-58 (2005-09-28)

This study demonstrates the use of Fourier transform infrared (FTIR) spectroscopy for monitoring both synthesis and hydrolysis reactions catalyzed by a recombinant amidase (EC 3.5.1.4) from Pseudomonas aeruginosa. The kinetics of hydrolysis of acetamide, propionamide, butyramide, acrylamide, benzamide, phenylalaninamide, alaninamide

A conductometric method for the assay of amidase and peptidase activities.

C R Hill et al.

Analytical biochemistry, 120(1), 165-175 (1982-02-01)

[Leucinamide specific cytosol leucine aminopeptidase].

T Kanno

Rinsho byori. The Japanese journal of clinical pathology, 30(5), 502-506 (1982-05-01)

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