scholarly journals Phosphate Partition in the Erythrocytes of Normal Newborn Infants and Infants with Erythroblastosis Fetalis. IV. Ion Exchange Chromatography

Blood ◽  
1963 ◽  
Vol 22 (5) ◽  
pp. 589-599 ◽  
Author(s):  
T. J. GREENWALT ◽  
S. A. MORELL ◽  
V. E. AYERS
Keyword(s):  
Ion Exchange ◽  
Pernicious Anemia ◽  
Perchloric Acid ◽  
Blood Cells ◽  
Newborn Infants ◽  
Severe Form ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Hemolytic Disease ◽  
High Level

Abstract Ion exchange chromatography was used to study perchloric acid extracts of the erythrocytes from the cord blood of normal infants and infants with erythroblastosis fetalis due to anti-D and, for comparison, the red blood cells of adults. Adenosine triphosphate, 2,3-diphosphoglycerate and the total phosphates were found to be highest in the infants with the most severe form of erythroblastosis fetalis. Evidence is given to show that these findings are not related to the relative immaturity of the erythrocytes in hemolytic discase of the newborn. No changes could be demonstrated in the partition of the intraerythrocytic phosphates in a patient with pernicious anemia before B12 therapy and at the height of the reticulocyte response. It is suggested that the high level of 2,3-diphosphoglycerate found in the erythrocytes in hemolytic disease due to anti-D may be due to alterations in the Embden-Meyerhof glycolytic pathway. The nature of the upheaval is not clear at present.

ION EXCHANGE CHROMATOGRAPHY OF THE FREE AMINO ACIDS IN THE PLASMA OF THE NEWBORN INFANT

PEDIATRICS ◽  
1965 ◽  
Vol 36 (1) ◽  
pp. 2-13
Author(s):  
Johanne C. Dickinson ◽  
Herman Rosenblum ◽  
Paul B. Hamilton
Keyword(s):  
Amino Acids ◽  
Ion Exchange ◽  
Newborn Infant ◽  
Free Amino Acids ◽  
Free Amino ◽  
Femoral Vein ◽  
Newborn Infants ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography

1. A micromethod for the determination of amino acids by ion exchange chromatography was applied to the quantitative determination of the free amino acids in 0.1 ml of plasma of the newborn infant. The precision of the method was in general within the range ± 5%. An interpretive analysis of a typical chromatogram is given. 2. Plasma was best stored at -68°C pending analysis; errors likely to arise on storage at -20°C and higher temperatures are pointed out. Some errors likely to arise in the preparation and storage of plasma protein free filtrates are also indicated. 3. Comparison of the free amino acids in the femoral vein plasma of 25 newborn infants was made with the literature values of the free amino acids in the plasma of adults. The differences noted were not great, but were apparently characteristic. On comparing heel puncture plasma, some amino acids were higher than in femoral vein plasma, but it was concluded that heel puncture plasma would be satisfactory for routine clinical purposes. Some possible sources of error which might explain the elevated amino acids in the heel puncture plasma were noted. 4. On comparison of newborn with 3-day-old infants, some changes in amino acid levels were noted. The changes were not great, but seemed to be characteristic and consistent. 5. A number of small peaks which have not been noted previously in plasma have been indicated on the chromatogram. They were not identified, but were mentioned to draw attention to the possibilities of hitherto unrecognized ninhydrin-positive components of plasma.

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

Review on the Application of Mixed-mode Chromatography for Separation of Structure Isoforms

2018 ◽  
Vol 20 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Tsutomu Arakawa
Keyword(s):  
Ion Exchange ◽  
Mixed Mode ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Charged State ◽  
Partial Structure ◽  
Reverse Phase ◽  
Oligomer Formation ◽  
Structure Rearrangement ◽  
Disulfide Scrambling

Proteins often generate structure isoforms naturally or artificially due to, for example, different glycosylation, disulfide scrambling, partial structure rearrangement, oligomer formation or chemical modification. The isoform formations are normally accompanied by alterations in charged state or hydrophobicity. Thus, isoforms can be fractionated by reverse-phase, hydrophobic interaction or ion exchange chromatography. We have applied mixed-mode chromatography for fractionation of isoforms for several model proteins and observed that cation exchange Capto MMC and anion exchange Capto adhere columns are effective in separating conformational isoforms and self-associated oligomers.

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