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P5267

Sigma-Aldrich

L-Proline p-nitroanilide trifluoroacetate salt

≥99% (TLC), suitable for ligand binding assays

Sinónimos:

N-(4-Nitrophenyl)pyrrolidine-2-carboxamide, P-pNA, Pro-pNA

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About This Item

Fórmula empírica (notación de Hill):
C11H13N3O3 · C2HF3O2
Número de CAS:
108321-19-3
Peso molecular:
349.26
MDL number:
MFCD00069671
UNSPSC Code:
12352209
eCl@ss:
32160406
PubChem Substance ID:
329820223
NACRES:
NA.26

product name

L-Proline p-nitroanilide trifluoroacetate salt, prolyl aminopeptidase substrate

assay

≥99% (TLC)

form

powder

technique(s)

ligand binding assay: suitable

color

white to yellow

storage temp.

2-8°C

SMILES string

OC(=O)C(F)(F)F.[O-][N+](=O)c1ccc(NC(=O)[C@@H]2CCCN2)cc1

InChI

1S/C11H13N3O3.C2HF3O2/c15-11(10-2-1-7-12-10)13-8-3-5-9(6-4-8)14(16)17;3-2(4,5)1(6)7/h3-6,10,12H,1-2,7H2,(H,13,15);(H,6,7)/t10-;/m0./s1

InChI key

KYRVEVYREUUAKH-PPHPATTJSA-N

General description

Proline p-nitroanilide (P-pNA) is a colorimetric substrate for prolyl aminopeptidase (proline iminopeptidase), an enzyme that releases proline from the N-terminus of small peptides.

Application

L-Proline p-nitroanilide trifluoroacetate salt has also been used as a monopeptide substrate for measuring the amidolytic activity of fibrillated peptide catalyst, PC4.
Proline p-nitroanilide (P-pNA) has been used as a substrate for prolyl aminopeptidase (proline iminopeptidase) from cabbage leaves.

Storage Class

11 - 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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Margarita Marinova et al.
Protein and peptide letters, 16(2), 207-212 (2009-02-10)
Chick-pea (Cicer arietinum L.) cotyledons are unique source of aminopeptidase - 8-9 U/g cotyledons was observed using L-leucine-p-nitroanilide as substrate. The aminopeptidase was purified (65 kDa, pI 4.8 ) reaching a specific activity of 220 U/mg at pH 7.0-7.2 and
Hongyu Yang et al.
World journal of microbiology & biotechnology, 32(11), 176-176 (2016-09-16)
Prolyl aminopeptidases are specific exopeptidases that catalyze the hydrolysis of the N-terminus proline residue of peptides and proteins. In the present study, the prolyl aminopeptidase gene (pap) from Aspergillus oryzae JN-412 was optimized through the codon usage of Pichia pastoris.
Paul J Lijnen et al.
Journal of the renin-angiotensin-aldosterone system : JRAAS, 6(2), 69-77 (2006-02-14)
To determine whether the aminopeptidase B inhibitor, arphamenine A, could affect collagen production and expression in control and TGF-ss1-treated cardiac fibroblasts. Cardiac fibroblasts from passage 2 from normal male adult rats were cultured to confluency and incubated with and without
Margarita Marinova et al.
Zeitschrift fur Naturforschung. C, Journal of biosciences, 63(1-2), 105-112 (2008-04-05)
Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2-7.5 for aminopeptidase activity and 8.0-8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by
Kazuyuki Hiwatashi et al.
Bioscience, biotechnology, and biochemistry, 68(6), 1395-1397 (2004-06-25)
We have found a novel prolyl aminopeptidase in Grifola frondosa. The enzyme was purified by DEAE-Sepharose CL-6B, Butyl-Toyopearl, Sephacryl S-100, and Mono-Q column chromatographies. The purified enzyme exists as a dimer and gives high activity toward L-proline-p-nitroanilide. The enzyme was
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