InChI key
CDOBGWIHUYXBJY-UHFFFAOYSA-N
InChI
1S/C12H12N2O.ClH/c13-8-12(15)14-11-6-5-9-3-1-2-4-10(9)7-11;/h1-7H,8,13H2,(H,14,15);1H
SMILES string
Cl.NCC(=O)Nc1ccc2ccccc2c1
assay
≥98% (TLC)
form
powder
technique(s)
protein purification: suitable
color
white to off-white
storage temp.
−20°C
Application
Glycine β-naphthylamide is used to identify, differentiate and characterize various amino acid β-naphthylamidase(s)/aminopeptidase(s).
P F Silveira et al.
Peptides, 22(12), 2137-2144 (2002-01-12)
Enzymatic cleavage of some peptides could be included among the mechanisms of water-electrolyte homeostasis. To test this hypothesis, the angiotensin-converting activity (ACE) of plasma and the L-cystine-di-beta-naphthylamidase activity (CAP) of plasma and of soluble and particulate fractions from different areas
Kiyoshi Ito et al.
Bioscience, biotechnology, and biochemistry, 67(1), 83-88 (2003-03-07)
Glycyl aminopeptidase was purified 600-fold from a cell extract of Actinomucor elegans by ammonium sulfate fractionation and sequential chromatography on DEAE-Toyopearl, Toyopearl HW65C, and FPLC-Superdex 200 HR, with recovery of 3.3% of the activity. The enzyme highly specifically hydrolyzed Gly-X
Anna Musidlowska-Persson et al.
Protein engineering, 16(12), 1139-1145 (2004-02-26)
It was shown recently that proline-beta-naphthylamidase from pig liver resembles the gamma-subunit of pig liver esterase (PLE), which could be functionally expressed in the yeast Pichia pastoris in recombinant form (rPLE). The gene encoding rPLE shares 97% identity with the
Endang Setyorini et al.
Journal of basic microbiology, 46(4), 294-304 (2006-07-19)
A halotolerant strain FP-133, able to grow at concentrations of 0-12.5% (w/v) NaCl, was isolated from a fish paste and identified as Bacillus subtilis . B. subtilis strain FP-133 produced an intracellular protease which showed catalytic activity under saline conditions.
T Takahashi et al.
The Journal of biological chemistry, 264(20), 11565-11571 (1989-07-15)
An enzyme hydrolyzing proline-beta-naphthylamide was purified to apparent homogeneity from porcine intestinal mucosa. The purified enzyme appears to consist of three identical subunit polypeptides with a molecular weight of about 58,000 each, associated noncovalently. The enzyme is a glycoprotein, and
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