Portable blood gas and electrolyte analyzer evaluated in a multiinstitutional study.

A recently introduced blood gas/electrolyte analyzer (SenDx 100((R)), renamed ABL70) intended for point-of-care, near-patient, or stat laboratory use was evaluated simultaneously in four different institutions and compared with three different laboratory bench analyzers with respect to imprecision, inaccuracy (assessed by tonometry), and patient-sample analyses. The analyzer is equipped with a sensor cassette and a reagent cartridge for 50, 100, or 200 analyses and 100 or more traditional quality-control measurements. One analysis requires 170 microL of whole blood and takes <90 s.

Isoforms of transferrin in psoriasis patients abusing alcohol.

The different isoforms of transferrin have been quantified by isoelectric focusing in the sera of psoriasis patients with and without a history of abusing alcohol. In both male and female psoriasis subjects abusing alcohol, there were significant increases in the 2-sialylated forms by comparison to the control subjects. Psoriasis patients who had no evidence of alcohol abuse had similar profile for the isoforms of transferrin to that of the controls.

Influence of transferrin glycans on receptor binding and iron-donation.

Human bi-bi-antennary transferrin (Tf) was partially deglycosylated by subsequently incubating with one or more of the following exoglycosidases: neuraminidase, beta-galactosidase or N-Acetyl-beta-D-glucosaminidase. Aglyco-Tf obtained from serum of a patient suffering from the Carbohydrate Deficient Glycoprotein syndrome was isolated. Receptor binding and the Tf and iron uptake capacities of the fully glycosylated-, partially deglycosylated- and aglyco-Tf were compared using the human hepatoma cell line PLC/PRF/5.

Isolation, renaturation and partial characterization of recombinant human transferrin and its half molecules from Escherichia coli.

Recombinant human transferrin as well as N- and C-terminal half-transferrins, produced in Escherichia coli, are deposited in inclusion bodies by the bacteria. The isolation and purification of the recombinant proteins from these inclusion bodies are described here. The amino acid compositions and N-terminal sequences of the proteins were determined, and found to be in agreement with the known protein structure of human serum transferrin.

Optimized bacterial production of nonglycosylated human transferrin and its half-molecules.

Transferrin is a glycoprotein functioning in iron transport in higher eukaryotes, and consists of two highly homologous domains. To study the function of the glycan residues attached exclusively to the C-terminal domain, we have constructed a plasmid allowing production of nonglycosylated human transferrin in Escherichia coli. By molecular biological and genetic techniques, production was stepped up to 60 mg/l.