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A6512
L-Arginin β-Naphthylamid -hydrochlorid
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About This Item
Empirische Formel (Hill-System):
C16H21N5O · HCl
CAS-Nummer:
Molekulargewicht:
335.83
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
PubChem Substanz-ID:
NACRES:
NA.83
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Assay
≥98% (TLC)
Qualitätsniveau
Form
powder
Löslichkeit
ethanol: 50 mg/mL, clear to slightly hazy, colorless to faintly yellow
Lagertemp.
−20°C
SMILES String
Cl.N[C@@H](CCCNC(N)=N)C(=O)Nc1ccc2ccccc2c1
InChI
1S/C16H21N5O.ClH/c17-14(6-3-9-20-16(18)19)15(22)21-13-8-7-11-4-1-2-5-12(11)10-13;/h1-2,4-5,7-8,10,14H,3,6,9,17H2,(H,21,22)(H4,18,19,20);1H/t14-;/m0./s1
InChIKey
WEVOXPYVEJEKIT-UQKRIMTDSA-N
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Yu-Chih Wang et al.
Veterinary microbiology, 142(3-4), 309-312 (2009-11-17)
Enrofloxacin (ER) resistant Actinobacillus pleuropneumoniae strains emerged in Taiwan in 2002. The mechanism of ER resistance in A. pleuropneumoniae has not yet been reported. A total of 48 A. pleuropneumoniae isolates were obtained from the lungs of pigs with pleuropneumonia
S Kawata et al.
Journal of biochemistry, 88(6), 1601-1605 (1980-12-01)
Porcine liver aminopeptidase B[EC 3.4.11.6] is highly specific for hydrolysis of beta-naphthylamides of basic L-amino acids; the Km values for L-arginine beta-naphthylamide and L-lysine beta-naphthylamide were 0.035 and 0.12 mM, respectively. The enzyme was inhibited by various alpha-amino acids. Among
H Kuramochi et al.
The Journal of antibiotics, 40(11), 1605-1611 (1987-11-01)
The action of ubenimex on aminopeptidase (APase) activity was studied in intact spleen cells and peritoneal macrophages from mice. Ubenimex strongly inhibited hydrolyzing activities against arginine-beta-naphtylamide (Arg-NA), Lys-NA and Pro-NA in both cells. Inhibition of hydrolysis of Leu-NA, Met-NA and
F Willenbrock et al.
The Biochemical journal, 227(2), 521-528 (1985-04-15)
The pH-dependences of kcat, Km and kcat./Km for the hydrolysis at 25 degrees C at I 0.1 of L-arginine 2-naphthylamide catalysed by cathepsin H from bovine spleen were determined in the pH range approx. 4-8. The pH-dependences of these kinetic
Substrate specificity and histochemical distribution of aminopeptidase in rat testis and epididymis.
T Matsuzawa
Endocrinologia japonica, 28(4), 469-475 (1981-08-01)
The substrate specificity of rat testicular and epididymal peptidase was investigated using chromogenic substrates, D. L-alanine-, L-arginine-, gamma-N-L-glutamine-, L-leucine-, D. L-methionine-, alpha-N-benzoyl-D. L-arginine-, and N-benzoyl-L-leucine-beta-naphthylamide. The histochemical distribution of peptidase activity demonstrated with these substrates was also investigated in the
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