Determination of Cellular Carbohydrates in Peanut Fungal Pathogens and Baker's Yeast by Capillary Electrophoresis and Electrochromatography

2001 ◽  
Vol 49 (11) ◽  
pp. 5265-5269 ◽  
Author(s):  
Minquan Zhang ◽  
Hassan A. Melouk ◽  
Kelly Chenault ◽  
Ziad El Rassi
Keyword(s):  
Capillary Electrophoresis ◽  
Fungal Pathogens ◽  
Baker’S Yeast ◽  
Baker's Yeast

Determination of glutathione in baker's yeast by capillary electrophoresis using methyl propiolate as derivatizing reagent

2013 ◽  
Vol 1300 ◽  
pp. 204-208 ◽  
Author(s):  
Eirini-Chrysanthi Tsardaka ◽  
Constantinos K. Zacharis ◽  
Paraskevas D. Tzanavaras ◽  
Anastasia Zotou
Keyword(s):  
Capillary Electrophoresis ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Methyl Propiolate ◽  
Derivatizing Reagent

Development of a Simplified Method for the Determination of Folates in Baker's Yeast by HPLC with Ultraviolet and Fluorescence Detection

2005 ◽  
Vol 53 (7) ◽  
pp. 2406-2411 ◽  
Author(s):  
Johan D. M. Patring ◽  
Jelena A. Jastrebova ◽  
Sofia B. Hjortmo ◽  
Thomas A. Andlid ◽  
I. Margaretha Jägerstad
Keyword(s):  
Fluorescence Detection ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Simplified Method

scholarly journals Radiochemical determination of a unique sequence around the reactive serine residue of a di-isopropyl phosphorofluoridate-sensitive plant carboxypeptidase and a yeast peptidase

1972 ◽  
Vol 128 (2) ◽  
pp. 229-235 ◽  
Author(s):  
D. C. Shaw ◽  
J. R. E. Wells
Keyword(s):  
Amino Acids ◽  
French Bean ◽  
Unique Sequence ◽  
Baker’S Yeast ◽  
Baker's Yeast ◽  
Serine Carboxypeptidase ◽  
Serine Residue ◽  
Radiochemical Determination ◽  
Bean Leaves

Phaseolain, a carboxypeptidase from French-bean leaves, and a partially purified peptidase from baker's yeast are inhibited by reaction with di-isopropyl phosphorofluoridate. Radioactive di-isopropyl [32P]phosphorofluoridate was used to show that the site of reaction is a unique serine residue and that the sequence of amino acids adjacent to the reactive serine is Glu-Ser-Tyr. This sequence is different from those of other ‘serine’ enzymes previously reported and, for phaseolain, represents an unequivocal example of a ‘serine’ carboxypeptidase.

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