Whole-blood and plasma amino acid analysis: gas-liquid and cation-exchange chromatography compared.

1980 ◽  
Vol 26 (2) ◽  
pp. 271-276 ◽  
Author(s):  
A M Lewis ◽  
C Waterhouse ◽  
L S Jacobs
Keyword(s):  
Amino Acid ◽  
Cation Exchange ◽  
Whole Blood ◽  
Amino Acid Analysis ◽  
Exchange Chromatography ◽  
Plasma Amino Acid ◽  
Cation Exchange Chromatography

scholarly journals Haemoglobins of the Adult Domestic Fowl Gallus Domesticus

1969 ◽  
Vol 22 (6) ◽  
pp. 1455 ◽  
Author(s):  
BA Moss ◽  
EOP Thompson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Cation Exchange ◽  
Amino Acid Analysis ◽  
Domestic Fowl ◽  
Exchange Chromatography ◽  
Gallus Domesticus ◽  
Cation Exchange Chromatography ◽  
Acidic Component ◽  
Dibasic Amino Acids

The haemoglobins of the adult domestic fowl were resolved by cation-exchange chromatography into two distinct components (designated Hb I and Hb II) in a ratio about 3 : 1. A third minor acidic component, Hb III, representing only 1 % of the total was also present. Hb I and Hb II and each of their globin subunits (0:1, pI; o:II, PII) were subjected to amino acid analysis. As reported by other workers, Hb II was found to have more of the dicarboxylic amino acids and less of the dibasic amino acids than Hb 1.

Bilirubin Interference In Plasma Amino Acid Analysis By Ion Exchange Chromatography

2018 ◽  
Vol 28 (9) ◽  
pp. 667-671
Author(s):  
Ayesha Hafeez ◽  
Safia Fatima ◽  
Aamir Ijaz Aamir Ijaz ◽  
Asif Ali Memon ◽  
Muhammad Waseem
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Analysis ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Plasma Amino Acid

Effect of sample instability on glycohemoglobin (HbA1) measured by cation-exchange chromatography.

1982 ◽  
Vol 28 (1) ◽  
pp. 195-198 ◽  
Author(s):  
M Simon ◽  
J D Hoover
Keyword(s):  
Confidence Interval ◽  
Cation Exchange ◽  
Whole Blood ◽  
Storage Condition ◽  
Exchange Chromatography ◽  
Cation Exchange Chromatography ◽  
Blood Samples ◽  
Whole Blood Samples

Abstract We compared results for glycohemoglobin obtained from fresh whole blood or separated erythrocyte samples with results obtained after storage. We judged the storage condition to be acceptable ("stable") if the glycohemoglobin results after storage were within the 95 confidence interval (+/- SD) of the results obtained for the specimens on the day of venipuncture. Hemolysates can validly be stored for five months at -70 degrees C. Whole-blood samples stored at 4 degrees C remain stable for four days; whole blood treated with heparin or EDTA (but not oxalate) is stable for seven days. At 30 degrees C, whole blood or erythrocytes from some donors are stable for one day, but after two days and seven days, results are frequently higher. We confirmed previous findings that the separated erythrocytes can be stored at -20 degrees C for at least seven days. In addition, we compared the elution profiles for stored samples showing increased values.

scholarly journals Chemical identity of tryptensin with angiotensin

1980 ◽  
Vol 187 (3) ◽  
pp. 647-653 ◽  
Author(s):  
K Arakawa ◽  
M Yuki ◽  
M Ikeda
Keyword(s):  
Amino Acid ◽  
Thin Layer ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Cation Exchange Chromatography ◽  
Human Plasma Protein ◽  
Plasma Protein Fraction ◽  
Layer Chromatography

Tryptensin, a vasopressor substance generated from human plasma protein fraction IV-4 by trypsin, has been isolated and the amino acid composition analysed. The procedures used for the isolation were: (a) adsorption of the formed tryptensin on Dowex 50W (X2; NH4+ form); (b) gel filtration through Sephadex G-25; (c) cation-exchange chromatography on CM-cellulose; (d) anion-exchange chromatography on DEAE-cellulose; (e) re-chromatography on CM-cellulose; (f) gel filtration on Bio-Gel P-2; (g) partition chromatography on high-pressure liquid chromatography. The homogeneity of the isolated tryptensin was confirmed by thin-layer chromatography and thin-layer electrophoresis. The amino acid analysis of the hydrolysate suggested the following proportional composition: Asp, 1; Val, 1; Ile, 1; Tyr, 1; Phe, 1; His, 1; Arg, 1; Pro, 1. This composition is identical with that of human angiotensin.

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