6042-04-2

Basic information

• Product Name: L-METHIONINE P-NITROANILIDE
• Synonyms: METHIONINE-PNA;L-METHIONINE 4-NITROANILIDE;L-METHIONINE P-NITROANILIDE;H-MET-PNA;methionine 4-nitroanilide;H-L-Met-pNA;L-Methionine 4-nitroanilide≥ 99% (HPLC);L-Met-pNA
• CAS NO: 6042-04-2
• Molecular Formula: C₁₁H₁₅N₃O₃S
• Molecular Weight: 269.32
• Product Categories: Amino Acids;I - Z;Modified Amino Acids
• Mol File: 6042-04-2.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 517.6°C at 760 mmHg
• Flash Point: 266.9°C
• Appearance: /
• Density: 1.333g/cm³
• Vapor Pressure: 8.06E-11mmHg at 25°C
• Refractive Index: 1.636
• Storage Temp.: −20°C
• CAS DataBase Reference: L-METHIONINE P-NITROANILIDE(CAS DataBase Reference)
• NIST Chemistry Reference: L-METHIONINE P-NITROANILIDE(6042-04-2)
• EPA Substance Registry System: L-METHIONINE P-NITROANILIDE(6042-04-2)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 6042-04-2(Hazardous Substances Data)

Usage

Chemical Properties

Light yellow crystalline powder

InChI:InChI=1/C11H15N3O3S/c1-18-7-6-10(12)11(15)13-8-2-4-9(5-3-8)14(16)17/h2-5,10H,6-7,12H2,1H3,(H,13,15)/t10-/m0/s1

Upstream product

• 2488-15-5 N-tert-butoxycarbonyl-L-methionine 
• 100-01-6 4-nitro-aniline 
• 84890-95-9 C₁₅H₂₇NO₆S 
• 70968-22-8 Boc-Met-pNA 

Downstream Products

• 15080-84-9 Phe-Met 
• 63-68-3 L-methionine 
• 85697-95-6 H-Tyr-Leu-Met-pNA*HCl 
• 82155-57-5 Suc-Tyr-Leu-Met-pNA 
• 85697-86-5 Boc-Tyr-Leu-Met-pNA 
• 85698-08-4 H-Leu-Met-pNA*HCl 
• 100-01-6 4-nitro-aniline 

Relevant articles and documents

Characterisation of the aminopeptidase from non-germinated winter rape (Brassica napus L.) seeds

Rapeseed plays a crucial role in food and fuel industry. Since aminopeptidases take part in many physiological processes in all organisms, it is important to learn their role and characteristics in economically relevant plants. Extracts of non-germinated winter rape seeds were screened for aminopeptidase activity. Substrate specificity, the influence of pH and temperature, as well as effect of protease inhibitors and chosen metal ions on the aminopeptidase activity were determined. The approximate molecular weight estimated by NATIVE-PAGE and SDS-PAGE electrophoresis was ～60 kDa. The partially purified enzyme as well as the aminopeptidases present in crude extract cleaved preferentially Phe-pNA. The activity profiles toward several substrates were also determined. Maximum activity was observed at pH 6.5 and temperature of 40 °C for Phe-pNA as a substrate. Two visible picks in the pH profile toward Phe-pNA, together with other results (IEF) suggest the presence of more than one aminopeptidase, having similar molecular mass. Much lower activity and broad pH profiles were observed for Leu- and Ala-pNA as substrates.

Synthesis of chromogenic substrates specific for human spleen fibrinolytic proteinase (SFP) and human leukocyte elastase (LE).

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