scholarly journals Fluorometric Determination of Tryptophan in Human Serum Using Phenylglyoxal.

1993 ◽  
Vol 9 (1) ◽  
pp. 25-27 ◽  
Author(s):  
Eijiro KOJIMA ◽  
Masaaki KAI ◽  
Yosuke OHKURA
2013 ◽  
Vol 181 (1-2) ◽  
pp. 239-248 ◽  
Author(s):  
Nahid Kamelipour ◽  
Afshin Mohsenifar ◽  
Meisam Tabatabaei ◽  
Tavoos Rahmani-Cherati ◽  
Kamyar Khoshnevisan ◽  
...  

2016 ◽  
Vol 183 (10) ◽  
pp. 2831-2836 ◽  
Author(s):  
Ting Tang ◽  
Jiang Ouyang ◽  
Lanshuang Hu ◽  
Linyan Guo ◽  
Minghui Yang ◽  
...  

1989 ◽  
Vol 54 (10) ◽  
pp. 2802-2808 ◽  
Author(s):  
Hana P. Mašková ◽  
George Kokotos ◽  
Chryssa Tzougraki ◽  
Tomislav Barth

A new fluorogenic substrate for the determination of the activity of human serum oxytocinase-cystine aminopeptidase (EC 3.4.11.3), H-Cys(Bzl)-NH-Meq, has been synthesized. The affinity of H-Cys(Bzl)-NH-Meq to oxytocinase was by two orders higher than that of the usually employed chromogenic substrates. The Michaelis constant of oxytocinase for this substrate was within the range of the optimum pH (7.0–7.5) 2.3.10-6 mol l-1, i.e. in the region of the affinity of the natural substrate, oxytocin. The concentration of dimethylsulfoxide used for the solubilization of H-Cys(Byl)-NH-Meq (<0.4%) did not influence adversely the course of the enzyme reaction as in the case of chromogenic substrates, where the concentrations of the organic solvent exceeded 3%.


Planta Medica ◽  
2010 ◽  
Vol 76 (12) ◽  
Author(s):  
A Copra-Janicijevic ◽  
E Sofic ◽  
L Klepo ◽  
A Topcagic ◽  
I Tahirovic ◽  
...  

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