Removing Substances from Blood by Affinity Chromatography
نویسندگان
چکیده
منابع مشابه
Removing substances from blood by affinity chromatography. I. Removing bilirubin and other albumin-bound substances from plasma and blood with albumin-conjugated agarose beads.
Substances such as bilirubin that bind tightly to plasma proteins cannot readily be removed from blood. We describe here the use of affinity chromatography as a new approach to the removal of proteinbound metabolites and toxins from blood. Agarose beads were coupled via cyanogen bromide to human serum albumin so as to contain 30-50 mg of albumin/g wet wt. Such beads, when exposed to plasma from...
متن کاملRemoving substances from blood by affinity chromatography. II. Removing bilirubin from the blood of jaundiced rats by hemoperfusion over albumin-conjugated agarose beads.
In vitro studies indicate that bilirubin and other albumin-bound substances can be efficiently removed from plasma by filtration over albumin-conjugated agarose beads. The effectiveness of this technique in vivo was investigated in rats by using a closed extracorporeal hemoperfusion system. Five Gunn rats whose endogenous bilirubin pool had been labeled with [(3)H]bilirubin and five Sprague Daw...
متن کاملPreparation of Plasminogen by Affinity Chromatography
Background: Plasminogen is one of the compounds derived from human plasma. Activation of plasminogen produces plasmin. Plasmin is able to lyse fibrinogen, fibrin, and some other human plasma proteins. The aim of the present work was to study the separation of human plasminogen by affinity chromatography using gel lysine Sepharose. Materials and Methods: Normal human plasma was used as the...
متن کاملpreparation of plasminogen by affinity chromatography
background: plasminogen is one of the compounds derived from human plasma. activation of plasminogen produces plasmin. plasmin is able to lyse fibrinogen, fibrin, and some other human plasma proteins. the aim of the present work was to study the separation of human plasminogen by affinity chromatography using gel lysine sepharose. materials and methods: normal human plasma was used as the start...
متن کاملPurification by Affinity Chromatography
The glycine receptor of rat spinal cord was solubilized with the nonionic detergent Triton X-100 and subsequently purified by affinity chromatography on aminostrychnine-agarose and wheat germ agglutininSepharose. An overall purification of 1950-fold was achieved. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and mercaptoethano1 revealed three glycine receptor-asso...
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ژورنال
عنوان ژورنال: Journal of Clinical Investigation
سال: 1974
ISSN: 0021-9738
DOI: 10.1172/jci107616