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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
Cathal S Mahon et al.
Microbiology (Reading, England), 155(Pt 11), 3673-3682 (2009-06-27)
Fungi are capable of degrading proteins in their environment by secreting peptidases. However, the link between extracellular digestion and intracellular proteolysis has scarcely been investigated. Mycelial lysates of the filamentous fungus Talaromyces emersonii were screened for intracellular peptidase production. Five
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
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