PubMed HealthSearch

PubMed · 5961064

A column method for deoxygenating human hemoglobin.

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

D F Wallach, M H Gail, C A Janeway. 1966. A column method for deoxygenating human hemoglobin.. https://doi.org/10.1016/0003-2697(66)90035-2

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Capillary and rotating-tube isoelectric focusing of a transmembrane protein, the human red cell glucose transporter.

The human red cell glucose transporter (Glut1) is a transmembrane protein. Monomeric Glut1 was purified by ion-exchange chromatography in the presence of the non-ionic detergent n-dodecyl octaoxyethylene (C12E8). For focusing, the ionic strength of the solution of C12E8-Glut1 complexes with co-purified lipids was lowered by dialysis, the detergent concentration was increased and carrier ampholytes were added. Focusing was done for 5 min at 3000 V in a methyl cellulose-coated glass capillary (50 microns I.D.). The anolyte H3PO4 was then replaced by NaOH for mobilization towards the anode. Absorbance monitoring at 280 nm showed two groups of zones at pH 6 and 8. Similarly, isoelectric focusing in a rotating quartz tube (3 mm I.D.) gave Glut1 zones at pH 5.5 and 8.0. Phosphorus analysis revealed that the Glut1 zone at pH 8 contained more phospholipids than did the other one. The above results together with previously determined and calculated isoelectric points (pI) of Glut1 indicate that the Glut1 at pH 8 is monomeric and that the zone at pH 5.5-6 represents oligomeric materials. The pI 8.0 at 22 degrees C applies for monomeric Glut1 in the absence of urea. The results exemplify that capillary isoelectric focusing of hydrophobic membrane proteins is possible.

Chromatography, Ion Exchange

Prospective clinical trial of high-purity factor VIII preparations in haemophiliacs.

An assessment of the immune status of both HIV-positive and HIV-negative haemophiliacs showed hypo-responsive and anergic patients in both groups. In HIV-positive patients, the immune suppression, in addition to HIV itself, may be caused by other viral infections such as all types of hepatitis as well as by factor VIII concentrates. The introduction of new technologies for preparing factor VIII concentrates led to the question of whether higher purity is associated with a protective effect on the immune system, which might improve the clinical course of HIV-positive patients. Factor VIII from two manufacturing processes was investigated, one prepared using an ion-exchange S/D step, and the other utilizing a monoclonal antibody step. It is concluded that changing the product, from the monoclonal antibody to the ion-exchange and vice versa in the HIV-negative patients does not cause a change in the immune profiles.

Chromatography, Ion Exchange

A simple and inexpensive chromatographic method for the purification of gamma-globulin from human serum.

Inexpensive cation- and anion-exchangers based on continuous polymer beds were prepared directly in a plastic syringe. These beds are unique in the sense that they are synthesized by a very simple and cost-effective procedure; for instance, no preparation of beads is required as in conventional methods. Highly purified gamma-globulin could be prepared easily by step-wise elution accomplished by forcing buffers of increasing salt concentration through the column with the aid of the plunger.

Chromatography, Ion Exchange