The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

Bz-Arg-OH     (2S)-2-benzamido-5- (diaminomethylideneamin...

Synonyms: Bz-L-Arg-OH, PubChem12889, CHEMBL25380, SureCN188590, AG-E-03036, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of NSC 118519


High impact information on NSC 118519


Biological context of NSC 118519


Associations of NSC 118519 with other chemical compounds


Gene context of NSC 118519

  • 4. Specific esterolytic activities of the kallikrein-like enzyme on N-tosyl-L-arginine methylester (TAME) and N-benzoyl-L-arginine ethylester (BAEE) are 109.5 and 23.6 mumol/min/mg, respectively [9].
  • The inhibition of bovine pancreatic trypsin by human alpha-1 proteinase inhibitor (alpha-1 PI) was studied under second-order conditions by continuously monitoring the fluorescence change due to the enzymatic hydrolysis of N alpha-benzoyl-L-arginine 7-amido-4-methyl-coumarin as substrate [10].
  • In addition, protease activity towards human serum albumin (Prot1), transferrin (Prot2) and N alpha-benzoyl-L-arginine 7-amido-4-methylcoumarin-hydrochloride (BAAMc; Prot3) were determined in a second GCF sample from the same site [11].
  • Activity blot analyses indicated one major proteinase activity that hydrolysed the trypsin substrate N-alpha-benzoyl-L-arginine rho-nitroanilide, and three major proteinase activities that hydrolysed the chymotrypsin substrate N-succinyl ala-ala-pro-phe rho-nitroanilide [12].

Analytical, diagnostic and therapeutic context of NSC 118519


  1. The heterodimeric protease clostripain from Clostridium histolyticum is encoded by a single gene. Dargatz, H., Diefenthal, T., Witte, V., Reipen, G., von Wettstein, D. Mol. Gen. Genet. (1993) [Pubmed]
  2. Characterization of an endoprotease from rat small intestinal mucosal secretory granules which generates somatostatin-28 from prosomatostatin by cleavage after a single arginine residue. Beinfeld, M.C., Bourdais, J., Kuks, P., Morel, A., Cohen, P. J. Biol. Chem. (1989) [Pubmed]
  3. Protease II from Escherichia coli. Purification and characterization. Pacaud, M., Richaud, C. J. Biol. Chem. (1975) [Pubmed]
  4. Characteristics of the association between prothrombin fragment 2 and alpha-thrombin. Myrmel, K.H., Lundblad, R.L., Mann, K.G. Biochemistry (1976) [Pubmed]
  5. Enzymic and physicochemical properties of Streptomyces griseus trypsin. Olafson, R.W., Smillie, L.B. Biochemistry (1975) [Pubmed]
  6. Isolation and characterization of papaya peptidase A from commercial chymopapain. Robinson, G.W. Biochemistry (1975) [Pubmed]
  7. Ethylene glycol and the thermostability of trypsin in a reverse micelle system. Stupishina, E.A., Khamidullin, R.N., Vylegzhanina, N.N., Faizullin, D.A., Zuev, Y.F. Biochemistry Mosc. (2006) [Pubmed]
  8. Continuous Proteolysis with a stabilized stabilized protease. I. Chemical stabilization of an alkaline protease. Boudrant, J., Cuq, J.L., Cheftel, C. Biotechnol. Bioeng. (1976) [Pubmed]
  9. Kallikrein-like enzyme from Crotalus ruber ruber (red rattlesnake) venom. Mori, N., Sugihara, H. Int. J. Biochem. (1988) [Pubmed]
  10. Kinetic analysis of enzyme inactivation under second-order conditions by use of substrate-to-product progress curves: application to the inhibition of trypsin by alpha-1 proteinase inhibitor. Ozer, I. Anal. Biochem. (1998) [Pubmed]
  11. Elevated conversion of alpha-2-macroglobulin to the complexed form in gingival crevicular fluid from adult periodontitis patients. Rosin, M., Benjamin, P., Rogers, P., Gibson, M., Van Leuven, F., Johnson, N.W., Curtis, M. J. Periodont. Res. (1995) [Pubmed]
  12. Digestive proteinases in Lasioderma serricorne (Coleoptera: Anobiidae). Oppert, B., Hartzer, K., Zuercher, M. Bull. Entomol. Res. (2002) [Pubmed]
  13. Some effects of zona pellucida glycoproteins and sulfated polymers on the autoactivation of boar sperm proacrosin and activity of beta-acrosin. Lo Leggio, L., Williams, R.M., Jones, R. J. Reprod. Fertil. (1994) [Pubmed]
WikiGenes - Universities