ABSTRACT
A new wet-state membrane characterization method, thermoporometry, was used to study the effect on membrane structure of commonly used sterilization methods for artificial kidney membranes. The porosity and pore size distribution of differently sterilized hollow fiber Hemophan hemodialysis membranes were determined. Also the effect of a glycerol treatment (before sterilization) on porosity and pore size distribution after sterilization was studied. Hemophan was found to have a pore size distribution of pores with radii between 1.5 and 12 nm. Most of the samples had a maximum pore volume at a pore radius of 2.5 nm, only the steam sterilized and non glycerol treated sample had a maximum pore volume at 1.5 nm. The porosity was found to vary between 14 and 31% and was dependent on the applied treatment.
Subject(s)
Biocompatible Materials , Cellulose/analogs & derivatives , Kidneys, Artificial , Membranes, Artificial , Sterilization/methods , Calorimetry , Ethylene Oxide , Glycerol , Humans , Porosity , SteamABSTRACT
The competitive adsorption of human serum albumin (HSA), human immuno-gamma-globulin (HIgG) and human fibrinogen (HFb) onto polystyrene (PS) at 20 degrees C and a pH of 7.35 (phosphate-buffered saline) was studied. Protein adsorption was studied using enzyme immunoassay. The results obtained with the immunoassay were compared with those obtained using radiolabelled proteins. Recent studies revealed that the adsorption behaviour of radiolabelled proteins onto surfaces differs from that of the non-labelled proteins, which may lead to misinterpretation of adsorption data. Differences in the adsorption behaviour of the labelled proteins as compared to non-labelled proteins can possibly be explained by the formation of modified proteins during the labelling procedure as shown by ion-exchange high-performance liquid chromatography (HPLC). The competitive adsorption of HSA, HIgG and HFb onto a PS latex was studied by measuring the depletion of proteins in solution. The decrease in protein concentration in solution was determined by HPLC techniques. A strong preferential adsorption of HFb was observed with maximum adsorption values of 0.6 micrograms/cm2.
Subject(s)
Blood Proteins/isolation & purification , Adsorption , Binding, Competitive , Fibrinogen/isolation & purification , Humans , Immunoglobulin G/isolation & purification , Iodine Radioisotopes , Latex , Microspheres , Polystyrenes , Serum Albumin/isolation & purificationABSTRACT
The adsorption behaviour of two commercial preparations of human IgG onto a polystyrene latex surface was studied. The adsorption isotherms obtained differed markedly; one preparation showed a plateau value of 0.4 microgram cm-2 which was reached at 0.1 g l-1, whereas the other preparation showed no plateau value within the concentration range studied (0.1-7.0 g l-1). Characterization by means of iso-electric focusing and HPLC also showed differences between the two preparations. No differences were observed when immuno-electrophoresis was carried out. These results stress the necessity for proper characterization of proteins used in adsorption studies.
Subject(s)
Immunoglobulin G , Immunosorbent Techniques , Latex , Polystyrenes , Adsorption , ProteinsABSTRACT
Human fibrinogen (HFB) was labeled with different radioactive labels (Technetium -99m and iodine -125) in various ways. Characterization by chromatographic and electrophoretic methods did not show differences between the labeled and the nonlabeled proteins. The effect of the label and the labeling method on the adsorption behaviour of 99mTc and 125I labeled HFB at a polystyrene surface was investigated. In all cases labeled HFB showed preferential adsorption as compared to nonlabeled HFB. The preferential adsorption was expressed in terms of a factor ø (van der Scheer et al. 1978a), which will be 1, when no preferential adsorption occurs. 99mTc - and 125I - HFB showed ø values from 1.48 - 1.88. It is concluded that only meaningful adsorption experiments with labeled proteins can be performed when the possible occurrence of preferential adsorption has been investigated by appropriate methods. The results of prior work on protein adsorption at biomaterials using radiolabeled proteins have to be reconsidered.
Subject(s)
Fibrinogen , Isotope Labeling , Adsorption , Humans , Iodine Radioisotopes , Polystyrenes , TechnetiumABSTRACT
In this study the cryo-unit is introduced as a new and useful instrument to investigate water-containing specimens with the SEM. Often water-containing biological specimens are studied, but in our case we used water-swollen polymer membranes. The results show that application of a cryo-unit permits the study of this material at low temperatures up to magnifications of about 10 000 times, while other techniques failed to give reproducible results.
