Abstract: Disclosed are specifically designed binding, "protein imaged" sorbents which reversibly bind with high specificity and affinity a preselected macromolecule, specifically a protein. The sorbents define one or more cavities which have a binding surface complementary in shape to the molecular surface of the macromolecule and a plurality of positively and negatively charged chemical moieties spatially distributed in a mirror image and charge inverse of a subset of the ionizable groups on the molecular surface of the macromolecule. Also disclosed are methods of producing such sorbents, useful over a range of conditions, for both preparative and analytical chromatographic separations or for use in various types of analyses.

Abstract: Disclosed are chemically-produced specific binding, "molecular imaged" sorbents which reversibly bind a preselected macromolecule by spatially matched multipoint interactions between functional groups synthesized on the surface of the sorbent and functional groups on the surface of the macromolecule. Also disclosed are methods of producing such sorbents. The sorbents typically are high surface area solids comprising surface binding regions which have charged groups, metal coordinating groups, hydrophobic moieties, or various combination thereof anchored thereto and spaced in the mirror image of complementary interactive groups on a surface of the macromolecule.

Abstract: Disclosed are chemically-produced specific binding, "molecular imaged" sorbents which reversibly bind a preselected macromolecule by spacially matched multipoint interactions between functional groups synthesized on the surface of the sorbent and functional groups on the surface of the macromolecule. Also disclosed are methods of producing such sorbents. The sorbents typically are high surface area solids comprising surface binding regions which have charged groups, metal coordinating groups, hydrophobic moities, or various combination thereof anchored thereto and spaced in the mirror image of complementary interactive groups on a surface of the macromolecule.

Abstract: Disclosed is a method for the rapid quantitative determination of low density lipoprotein (LDL) in a biological fluid sample containing LDL, very low density lipoprotein (VLDL) and high density lipoprotein (HDL). The sample is first passed through a matrix to bind LDL to the matrix. The LDL is then eluted from the matrix differentially from VLDL and HDL. A parameter representative of the concentration of a solute exiting the matrix during the interval when LDL is eluted is then determined, wherein the parameter is proportional to the amount of the LDL in the sample. The parameter may be determined, e.g., by electronically integrating under a spectrophotometrically detected peak of eluted LDL.

Abstract: A method of derivatizing a chromatography matrix having a hydrophobic surface involves reacting the hydrophobic surface with a halosulfonating agent to produce a significant amount of halosulfone groups covalently bonded onto the surface. Sulfonamide bonds then are formed between these halosulfone groups and a group of amine functions on a polyaminated polymer to produce a pellicular anion exchange layer covalently bonded to the surface. The resulting layer is stable in the absence of cross-links between the molecules of the polyaminated polymer.

Abstract: Disclosed are chemically-produced specific binding, "molecular imaged" sorbents which reversibly bind a preselected macromolecule by spacially matched multipoint interactions between functional groups synthesized on the surface of the sorbent and functional groups on the surface of the macromolecule. Also disclosed are methods of producing such sorbents. The sorbents typically are high surface area solids comprising surface binding regions which have charged groups, metal coordinating groups, hydrophobic moities, or various combination thereof anchored thereto and spaced in the mirror image of complementary interactive groups on a surface of the macromolecule.

Abstract: Disclosed are pellicular materials useful in contact with proteins and as chromatography media. Rigid, inert, hydrophobic, polymeric materials are exposed to a solution comprising a solute defining plural interspersed hydrophobic and hydrophilic domains. The solute molecules adsorb onto the surface of the substrate by hydrophobic - hydrophobic interaction with their hydrophilic domains extending outwardly away from the surface into the solution. The molecules are then crosslinked in place to produce a solvent and pH resistant coating which presents a hydrophilic surface sufficient to mask hydrophobic regions therebeneath. The multidomain adsorbing compounds may comprise reactive groups which subsequently can be derivatized using conventional techniques to produce chromatography materials useful for conducting affinity, size exclusion, cationic exchange, anionic exchange, neutral hydrophobic interaction, and other forms of chromatographic separations.