Automated Determination of Free Amino Groups in Serum and Plasma Using 2,4,6-Trinitrobenzene Sulfonate

1969 ◽  
Vol 15 (9) ◽  
pp. 891-901 ◽  
Author(s):  
D W Palmer ◽  
T Peters

Abstract A simple automated method is described for determining the level of total free amino acids in the blood. The method utilizes the AutoAnalyzer, and is based on the formation of colored complexes by uniting free amino groups with 2,4,6-trinitrobenzene sulfonate (TNBS). Proteins do not interfere because the free amino acids are first separated by dialysis. Characteristics of the reaction and potential clinical applications of the procedure are discussed.

2019 ◽  
Vol 146 ◽  
pp. 56-65 ◽  
Author(s):  
Emilia Waraksa ◽  
Konrad Kowalski ◽  
Rafał Rola ◽  
Ewa Kłodzińska ◽  
Tomasz Bieńkowski ◽  
...  

1990 ◽  
Vol 42 (3) ◽  
pp. 288-293 ◽  
Author(s):  
M.J.Medina Hernández ◽  
R.M.Villanueva Camañas ◽  
M.C.García Alvarez-Coque

1994 ◽  
Vol 61 (3) ◽  
pp. 437-440 ◽  
Author(s):  
Yvette Bouton ◽  
Remy Grappin

Free amino groups produced during cheese ripening are used to indicate the extent of cheese proteolysis. Several studies have shown a high correlation between the level of free amino acids and the flavour of Gouda (Aston et al. 1983) or Comté (Grappin & Berdagué, 1989). Measurement of the level of free amino acids seems useful for the investigation of flavour chemistry in cheese (Lemieux et al. 1990). The determination of N fractions is often used to estimate the degree of proteolysis in cheese, but since this procedure is laborious and time consuming several attempts have been made to replace it by more rapid methods (Ardö & Meisel, 1991). Since its introduction by Satake et al. (1960), the 2,4,6-trinitrobenzenesulphonic acid (TNBS) method has been widely used for the determination of free amino groups. Because TNBS does not react with the imino groups of histidine and proline or the hydroxyl groups of tyrosine, serine or threonine, it has been accepted as a selective reagent for primary amino groups (Burger, 1974). Measurement of N by Kjeldahl in the phosphotungstic acid (PTA)–sulphuric acid extract (Gripon et al. 1975) estimates the N of free amino acids and low molecular mass peptides. The purpose of this study was to compare the TNBS and PTA-soluble N methods in order to find out whether the TNBS procedure can replace that of PTA-soluble N in the determination of a cheese proteolysis index.


1950 ◽  
Vol 182 (1) ◽  
pp. 29-37
Author(s):  
P.E. Schurr ◽  
H.T. Thompson ◽  
L.M. Henderson ◽  
C.A. Elvehjem

2001 ◽  
Vol 68 (1) ◽  
pp. 117-129 ◽  
Author(s):  
ABDELGHANI OUMER ◽  
PILAR GAYA ◽  
ESTRELLA FERNÁNDEZ-GARCÍA ◽  
RAÚL MARIACA ◽  
SONIA GARDE ◽  
...  

Hispánico cheese, a semi-hard Spanish variety, was manufactured from a mixture of pasteurized cows' and ewes' milks (4[ratio ]1) using a commercial mesophilic LD-type starter comprising Lactococcus lactis subsp. cremoris, Lc. lactis subsp. lactis, Lc. lactis subsp. lactis var diacetylactis and Leuconostoc mesenteroides subsp. cremoris. Varying amounts (0–1·0 g/kg) of an Enterococcus faecalis INIA 4 culture in milk were added as a bacteriocin-producing adjunct. Differences in pH between cheeses manufactured with and without the bacteriocin producer did not exceed 0·11 pH units. Starter lactococci lost viability more rapidly in cheeses made with the bacteriocin producer, which reached counts of up to 6×107 cfu/g during ripening. Aminopeptidase activity in 1-d-old cheese made from milk inoculated with 1·0 g bacteriocin-producing culture/kg was twice that in control cheese. Degrees of overall proteolysis and levels of total free amino acids in 45-d-old cheese made with 1·0 g bacteriocin-producing culture/kg were 1·80-fold and 2·17-fold those in control cheese of the same age. Inoculating milk with 1·0 g/kg bacteriocin-producing culture reduced the level of hydrophobic peptides in the resultant cheese, increased the concentrations of 3-methyl-1-butanal, diacetyl and acetoin, and resulted in the highest scores for flavour quality and flavour intensity throughout ripening.


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