scholarly journals Properties of human tissue isoferritins

1978 ◽  
Vol 173 (3) ◽  
pp. 969-977 ◽  
Author(s):  
M Wagstaff ◽  
M Worwood ◽  
A Jacobs
Keyword(s):  
Ion Exchange ◽  
Isoelectric Focusing ◽  
Iron Content ◽  
Iron Uptake ◽  
Human Liver ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Normal Tissues ◽  
Multiple Blood ◽  
Liver Ferritin

1. Human liver ferritin was separated by preparative isoelectric focusing into six fractions. 2. Except for the least acidic fraction the reactivity with antibody against spleen ferritin increased with rising pI, but with antibody against heart ferritin the reactivity decreased. 3. The highest iron content was found in the most acidic isoferritins and progressively decreased with rising pI. 4. Iron uptake was studied in apoferritin prepared from heart and liver ferritin fractions separated by ion-exchange chromatography. There was good correlation between the rate of iron uptake and pI. The most acidic fractions took up iron more rapidly than did the more basic ones. 5. Ferritin was prepared from heart, liver, spleen and kidney. There was little difference on isoelectric focusing between ferritin obtained from normal tissues and the corresponding iron-loaded tissues from patients who had received multiple blood transfusions. The iron-loaked heart ferritin invariably contained relatively more of the basic isoferritins. Normal and iron-overloaded heart ferritins were separated into isoferritin fractions by ion-exchange chromatography, and in each case there was a fall in iron content as the pI increased. The iron content of ferritin from the iron-overloaded heart was higher throughout than that from normal heart. 6. There is a relationship between the rate of iron uptake by apoferritin and pI, and this probably accounts for the variation in iron content of the isoferritins found in human liver and heart.

Iron and Isoferritins in Iron Overload

1982 ◽  
Vol 62 (5) ◽  
pp. 529-540 ◽  
Author(s):  
M. Wagstaff ◽  
M. Worwood ◽  
A. Jacobs
Keyword(s):  
Ion Exchange ◽  
Iron Overload ◽  
Isoelectric Point ◽  
Iron Content ◽  
Iron Uptake ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Subunit Composition ◽  
Normal Heart ◽  
Normal Tissues

1. The ferritin content of iron-overloaded tissues was higher than that of normal tissues. There was also an increased iron content of ferritin extracted from these tissues. 2. In the limited number of tissues that we examined haemosiderin deposition appeared to be greater in the iron-overloaded livers than in the iron-overloaded spleens. 3. Ferritins extracted from iron-overloaded liver, spleen and kidney had similar properties to those extracted from the corresponding normal tissues. 4. Ferritin from iron-overloaded heart had a greater proportion of more basic isoferritins than had ferritin from normal heart. 5. Immunoreactivity to heart and spleen ferritin antibodies, subunit composition, iron content and rate of iron uptake of both unfractionated ferritin and isoferritin fractions separated by ion exchange chromatography were related to the isoelectric point.

scholarly journals Heterogeneity in tissue ferritins displayed by gel electrofocusing

1974 ◽  
Vol 141 (3) ◽  
pp. 627-632 ◽  
Author(s):  
James W. Drysdale
Keyword(s):  
Ion Exchange ◽  
Human Liver ◽  
Structural Heterogeneity ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Human Liver Ferritin ◽  
Liver Ferritin ◽  
Horse Spleen Ferritin

1. Horse spleen ferritin and human liver ferritin were examined by gel electrofocusing under conditions that demonstrated equilibrium focusing. Both ferritins were resolved into multiple isoferritins. Both families of isoferritins were separable from one another. 2. Horse spleen ferritin was also resolved into five components by ion-exchange chromatography on DEAE-Sephadex A-50. Each of the major chromatographic fractions contained only a few of the isoferritins seen on gel electrofocusing. Each chromatographic fraction corresponded to different portions of the isoferritin profile. 3. These results indicate that the heterogeneity seen in many ferritins by gel electrofocusing represents structural heterogeneity in the ferritin population as isolated from the tissues.

scholarly journals Heat-stable enterotoxins from Escherichia coli P16

1980 ◽  
Vol 28 (3) ◽  
pp. 1038-1040
Author(s):  
M N Burgess ◽  
N A Mullan ◽  
P M Newsome
Keyword(s):  
Escherichia Coli ◽  
Ion Exchange ◽  
Isoelectric Focusing ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Infant Mouse ◽  
Heat Stable

Escherichia coli P16 infant mouse active heat-stable enterotoxin may be fractionated into two distinct active moieties by ion-exchange chromatography, Sephadex G-25 chromatography, and isoelectric focusing.

scholarly journals The N-acetylhexosaminidase components of the ram testis and epididymis

1973 ◽  
Vol 133 (3) ◽  
pp. 593-599 ◽  
Author(s):  
Sarah Bullock ◽  
Bryan Winchester
Keyword(s):  
Molecular Weight ◽  
Ion Exchange ◽  
Isoelectric Focusing ◽  
Catalytic Properties ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Multiple Forms ◽  
The Individual

Three and four N-acetylhexosaminidase components, from ram testis and epididymis respectively, have been separated by ion-exchange chromatography on DEAE-cellulose. Although they all have the same molecular weight (approx. 140000) and very similar catalytic properties towards the synthetic substrates, 4-methylumbelliferyl N-acetyl-β-glucosaminide and N-acetyl-β-galactosaminide, isoelectric focusing of the individual components showed that each had a distinct pI value. Isoelectric focusing has also been used to demonstrate the occurrence of multiple forms in ejaculated ram semen.

Correlating charge heterogeneity data generated by agarose gel isoelectric focusing and ion exchange chromatography methods

2018 ◽  
Vol 1073 ◽  
pp. 1-9 ◽  
Author(s):  
Babita Saxena Parekh ◽  
Arvind Srivastava ◽  
Shanmuuga Sundaram ◽  
Ming Ching-Heish ◽  
Joel Goldstein ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Isoelectric Focusing ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Agarose Gel ◽  
Charge Heterogeneity ◽  
Gel Isoelectric Focusing

Separation and Characterization of Two Fibrinolytic Inhibitors from Human Placenta

1971 ◽  
Vol 25 (03) ◽  
pp. 580-589 ◽  
Author(s):  
M Uszynski ◽  
U Abildgaard
Keyword(s):  
Molecular Weight ◽  
Ion Exchange ◽  
Isoelectric Focusing ◽  
Basic Protein ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Coagulation Inhibitor ◽  
Tissue Thromboplastin

SummaryProcedures for the separation of two inhibitors of the activation of plasminogen to plasmin by urokinase are described. Tissue thromboplastin was removed by adsorption to Al(0H)3 gel followed by ultracentrifugation. Plasminogen, plasminogen activator, a coagulation inhibitor and hemoglobin were removed by ion exchange chromatography (CM- or DEAE-Sephadex with NaCl gradients). The minor UK inhibitor is a relative basic protein with a pI of about 5.8. The major inhibitor was purified further by isoelectric focusing, preparative electrophoresis in polyacrylamide gel, and gel filtration. This inhibitor has α1-motility, the pI is about 5.2, and the molecular weight about 100,000. It inactivates urokinase progressively, but does not inhibit streptokinase, plasmin or thrombin.

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