A new dipeptide naphthylamidase hydrolyzing glycyl-prolyl-β-naphthylamide

@article{HopsuHavu2004AND,
  title={A new dipeptide naphthylamidase hydrolyzing glycyl-prolyl-$\beta$-naphthylamide},
  author={V{\"a}in{\"o}K. Hopsu-Havu and George G. Glenner},
  journal={Histochemie},
  year={2004},
  volume={7},
  pages={197-201}
}
Material and Methods Na-Cbz-Glycyl-DL-Prolyl-fi-Naphthylamide. Na-Cbz-Gly-DL-Pro (2g) and 2-naphthylamine (1 g) were dissolved in 50 ml of tetrahydrofuran at -10 ~ C. To this solution was added 1.35 g N,Nl-dicyclohexylcarbodiimide and with mechanical stirring the solution was brought slowly to 25 o C with stirring continued for 16 hours. The precipitated urea was removed by filtration and the filtrate evaporated to dryness in vacuo. The amorphous residue was extracted with dichloromethane and… 

Studies on glycyl-proline naphthylamidase

  • Z. Lojda
  • Biology, Medicine
    Histochemistry
  • 2004
Glycyl-proline naphthylamidase (Gly-Pro-Nase) was discovered in peripheral blood lymphocytes of healthy adult humans and in mini-pigs and it was demonstrated neither in the blastically transformed lymphocytes (after phytohemagglutinine stimulation) nor in epithelial lymphocyte of the human jejunum.

A sulphydryl-dependent and chloride-activated peptidase (cathepsin C) that hydrolyses alanyl-alanine naphthylamide

The enzyme was shown to be optimally active at pH 5.0–6.0, dependent on sulphydryl groups, and activated by chloride ions, and was heat stable at 60°C, and its isoelectric point was between 4.8 and 6.0.

Studies on dipeptidyl(amino)peptidase IV (glycyl-proline naphthylamidase)

  • Z. Lojda
  • Biology, Chemistry
    Histochemistry
  • 2004
The contribution of DAP IV activity of the capillary endothelium to the total DAPIV activity in a particular organ is decisive in the myocardium, striated muscle, aorta and lung; it represents about one half of the total activity in spleen and pancreas and is less expressed in the liver, intestine and particularly in the kidney.

Periplasmic form of dipeptidyl aminopeptidase IV from Pseudoxanthomonas mexicana WO24: purification, kinetic characterization, crystallization and X-ray crystallographic analysis.

Initial phases were determined by the molecular-replacement method using Stenotrophomonas maltophilia DPP IV (PDB entry 2ecf) as a template and refinement of the structure is in progress.

Peptidasen II. Zur Lokalisation der Dipeptidylpeptidase IV (DPP IV). Histochemische und biochemische Untersuchung

The results obtained for DPP IV suggest a peptidylpeptidase which seems to be involved in other metabolic processes beside the degradation of collagen, and confirms the species- and organ-dependent differences revealed by histochemistry.

Development of a fluorogenic small substrate for dipeptidyl peptidase-4

Results suggest that H-Gly-Pro-1 could be used as fluorophore in OFF–ON-type fluorogenic probes.

Review The prolyl oligopeptidase family

The recent crystal structure deter- mination of prolyl oligopeptidase has shown that the enzyme contains a peptidase domain with an a/b hydrolase fold, and its catalytic triad is covered by the central tunnel of an unusual seven-bladed b-propeller.

The evolution of proteinase substrates with special reference to dipeptidylpeptidase IV

SummaryThe design and development of specific substrates for proteolytic enzymes is reviewed. Particular attention is given to substrates containing the leaving groups 4-methoxy-2-naphthylamide (MNA)
...

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