Gly pro p nitroanilide hydrochloride

Manufactured by Merck Group

Sourced in United States

Gly-Pro p-nitroanilide hydrochloride is a laboratory reagent used for the detection and quantification of enzymatic activity. It serves as a substrate for various proteolytic enzymes, particularly those that cleave peptide bonds involving proline residues. The compound consists of the amino acid glycine coupled to proline, with a p-nitroaniline moiety attached. Upon enzymatic hydrolysis, the release of p-nitroaniline can be measured spectrophotometrically, providing a quantitative assessment of the enzyme's activity.

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Gly-Pro-p-nitroanilide Hydrochlorides

5 protocols using gly pro p nitroanilide hydrochloride

Enzymatic Inhibition of Angiotensin-Converting Enzyme

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Portuguese oysters (Crassostrea angulata) were purchased from Penghu Island, Taiwan. They were packed in a box with ice and sent to the laboratory by freight transport. Pepsin (from porcine gastric mucosa), bromelain (from pineapple stem), and papain (from papaya) were obtained from Sigma-Aldrich (St. Louis, MO, USA). The angiotensin I converting enzyme (ACE) from rabbit lung (≥2 units/mg), N-(3-[2-furyl]-acryloyl)-phenylalanyl glycyl glycine (FAPGG), Dipeptidyl Peptidase IV (DPP-IV) from human recombinant (≥1 unit/mg), and Gly-Pro p-nitroanilide hydrochloride (≥99%) were also acquired from Sigma-Aldrich, USA. All chemical reagents used were of analytical grade.

Gomez H.L., Peralta J.P., Tejano L.A, & Chang Y.W. (2019). In Silico and In Vitro Assessment of Portuguese Oyster (Crassostrea angulata) Proteins as Precursor of Bioactive Peptides. International Journal of Molecular Sciences, 20(20), 5191.

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Gly-Pro p-Nitroanilide Assay

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Grafts in culture (or unseeded controls) were removed from culture and washed in PBS three times. Gly-Pro p-nitroanilide hydrochloride (Sigma cat.no. G0513) was dissolved in PBS at a concentration of 1.5mM and added to the grafts for 1 hour at 37°C before supernatant was collected. Optical density (415nm) was measured in duplicate and concentration determined by comparison to a 4-nitroaniline (Sigma cat.no. 185310) standard curve.

Laween M., Isobel M., Sara C., Weston A.E., Riana G., Lucinda T., Peter F., Michael O., Anna K., Anna B., Laura N., Nikolaos A., Elizabeth H., Julia K., Tedeschi A.M., Pellegata A.F., Susanna E., Alessandro A.P., Lucy C., Nikhil T., Thomas G.M., Simon E., Paola B., De Coppi P, & Li V.S. (2020). Engineering transplantable jejunal mucosal grafts using patient-derived organoids from children with intestinal failure. Nature medicine, 26(10), 1593-1601.

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Peptidase Activity Assay Protocol

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Porcine pepsin (EC 3.4.23.1, from porcine gastric mucosa, 3850 U mg⁻¹ protein), pancreatin from porcine pancreas (4 × USP specifications (5.46 U mg⁻¹ based on trypsin activity), EC 232-468-9), Dipeptidyl Peptidase IV (DPP-IV from porcine kidney, EC 3.4.14.5, ≥10 U mg⁻¹ protein), Gly-Pro-p-nitroanilide hydrochloride, Angiotensin Converting Enzyme (ACE from rabbit lung, EC 3.4.15.1), and all other reagents were purchased from Sigma-Aldrich (Sigma-Aldrich, Steinheim, Germany). The Active Glucagon-Like Peptide RIA kit (Cat.# GLP1A-35HK) was purchased from Merck Millipore (Merck-Millipore, Darmstadt, Germany). The Gastrin/CCK kit was purchased from CisBio (CisBio, Saclay, France). Human IL-8/CXCL8 Quantikine ELISA Kit (D8000C) was purchased from R&D Systems (R&D Sytems, Minneapolis, MN, USA).

Dugardin C., Cudennec B., Tourret M., Caron J., Guérin-Deremaux L., Behra-Miellet J., Lefranc-Millot C, & Ravallec R. (2020). Explorative Screening of Bioactivities Generated by Plant-Based Proteins after In Vitro Static Gastrointestinal Digestion. Nutrients, 12(12), 3746.

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Enzymatic Characterization of Pancreatic Biomolecules

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Pancreatic α-amylase, human recombinant DPP-IV, lipase from porcine pancreas (type VI-S, ≥20,000 U/ mg of protein), CE from porcine pancreas (~35 U/ mg), p-nitrophenyl-α-d-maltohexaoside, gly-pro-pnitroanilide hydrochloride, and p-nitrophenyl butyrate were purchased from Sigma Aldrich. All the chemicals, solvents, and standards used for SDS-PAGE were purchased from Bio-Rad and those for HPLC were purchased from Sigma Aldrich and were of analytical grade.

Mudgil P., Redha A.A., Nirmal N.P, & Maqsood S. (2023). In vitro antidiabetic and antihypercholesterolemic activities of camel milk protein hydrolysates derived upon simulated gastrointestinal digestion of milk from different camel breeds. Journal of dairy science, 106(5).

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Enzymatic Hydrolysis of Canary Seeds

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Hairless canary seeds of the CDC Cibo variety were purchased from a commercial vendor (Canpulse Foods LTD, Saskatoon, SK, Canada). Alcalase® (protease from Bacillus licheniformis, EC 3.4.21.62) and Lecitase® Ultra (Phospholipase A1 from Aspergillus oryzae) were purchased from Sigma Aldrich (St. Luis, MO, USA). Human Angiotensin-Converting Enzyme (ACE), Dipeptidyl Peptidase IV (DPP-IV, ≥ 4500 units/ μg protein), and their substrates Gly-Pro p-nitroanilide hydrochloride, and Hippuryl-L-Histidyl-L-Leucine (HHL), respectively, were all purchased from Sigma Aldrich (St. Louis, MO, USA). All chemicals used in this study were reagentgrade obtained by three leading companies VWR International (Radnor, PA, USA), Sigma Aldrich (St. Louis, MO, USA), and Thermo Fisher Scientific (Waltham, MA, USA).

Urbizo-Reyes U., Aguilar-Toalá J.E., & Liceaga A.M. (2021). Hairless canary seeds (Phalaris canariensis L.) as a potential source of antioxidant, antihypertensive, antidiabetic, and antiobesity biopeptides. Food Production Processing and Nutrition, 3(1).

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