High impact information on Val-Leu-Arg-p-nitroanilide

• Finally, crotalase exhibits substrate specificity not only for the thrombin chromogenic substrate S-2238 but also for the kallikrein substrates S-2302 and S-2266 [1].
• The isolated enzyme liberated kinins from kininogen II of low molecular weight (sp. act. 14 ng kinins/min X mg) and p-nitroaniline (pNA) from the substrate S-2266 (sp. act. 1.23 nmoles pNA/min X mg); it was inhibited by aprotinin, benzamidine and rat urinary antikallikrein antibody but not by ovomucoid [2].
• IIa was a potent chemotactic agent for PMNs (p less than or equal to 0.0121) and stimulated the release of TK (p less than or equal to 0.0001) as determined by hydrolysis of S-2266 [3].
• Seminal plasma kallikrein activity was measured with the aid of the specific chromogenic substrate S-2266 [4].
• The activity of tissue kallikrein was determined from a random untimed urine sample using a selective, synthetic chromogenic tripeptide substrate having the sequence H-D-Val-Leu-Arg-pNA (S-2266) [5].

Biological context of Val-Leu-Arg-p-nitroanilide

• An enzyme immunoassay for the determination of human urinary kallikrein has been developed and is compared with other human urinary kallikrein assays such as radioimmunoassay, dog blood pressure assay, rat uterus test after kinin liberation and synthetic substrate(20) tests (AcPheArgOEt and S-2266) [6].

Anatomical context of Val-Leu-Arg-p-nitroanilide

• In this study, we demonstrate (using the chromogenic tripeptide substrate S 2266) that the renal cell line A6 from Xenopus laevis secretes a kallikrein-like enzyme [7].

Associations of Val-Leu-Arg-p-nitroanilide with other chemical compounds

• LV-Ka was active upon the kallikrein substrates S-2266 and S-2302 (specific activity=13.0 and 31.5 U/mg, respectively; crude venom=0.25 and 6.0 U/mg) but had no proteolytic effect on dimethylcasein and insulin B chain [8].

Gene context of Val-Leu-Arg-p-nitroanilide

• Urinary kallikrein activity in rats and man was measured by an amidolytic assay using the chromogenic tripeptide D-valyl-leucyl-arginine-p-nitroanilide (S 2266) [9].
• Esterase A1 showed no amidase activity towards the substrate H-D-Val-Leu-Arg-p-nitroanilide [10].
• It is concluded that S-2266 is an accurate substrate for the assay of glandular kallikrein in human mixed saliva; that the inclusion of SBTI in the assay mixture is needed to inhibit non-kallikrein proteases that may also hydrolyse the synthetic substrate; and that prekallikrein is present in mixed saliva [11].
• This enzyme was found to hydrolyze casein and various chromogenic peptide substrates; highest activity occurred with H-D-Val-Leu-Arg-p-nitroanilide, reported to be a specific substrate for human glandular kallikreins [12].

Analytical, diagnostic and therapeutic context of Val-Leu-Arg-p-nitroanilide

• Kallikrein activity was determined with S-2266 substrate and by radioimmunoassay of kinin released [13].
• Urinary kallikrein activity was measured by the enzymatic hydrolysis of synthetic chromogenic substrate S-2266, and urinary electrolytes were measured by flame photometry [14].

References