Lysine 4-nitroanilide 

Lysine 4-nitroanilide is an amino acid derivative used in studies of enzymology. Two major arylamidase activities were isolated from particle-free supernatant of rat heart by DEAE-Sephadex chromatography. Although both enzymes hydrolyze L-leucine 4-nitroanilide, only the peak II enzyme does so. A third, minor peak (Ia) contains the enzyme active primarily toward L-lysine 4-nitroanilide. The molecular weights of the enzymes in peaks I and II are approximately 257,000 and 105,000, respectively. The optimum pH for the peak I enzyme is approximately pH 7.0, while that for the peak II enzyme is between 7.0 and 8.0. Both enzymes are inhibited by puromycin, p-hydroxymercurybenzoate, catechol, and divalent metal ions. Addition of dithiothreitol stimulates both activities. Dialysis against catechol resulted in inhibition of both peak I and II enzymes, but dialysis against EDTA inhibited only the peak II enzyme.

266.30

C₁₂H₁₈N₄O₃

6184-11-8

O=C(NC1=CC=C([N+]([O-])=O)C=C1)C(N)CCCCN

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Separation and properties of two arylamidases from rat cardiac-muscle extracts