Preoperative middle meningeal artery embolization in the treatment of organized chronic subdural hematoma.

Organized chronic subdural hematoma is a rare form of chronic subdural hematoma. The optimal treatment method is still controversial. Preoperative middle meningeal artery embolization and craniotomy are effective methods for chronic subdural hematoma.

Selective opening of airholes in photonic crystal fiber.

We introduce a femtosecond-laser-based technique for selective opening of airholes in photonic crystal fibers (PCFs). With this technique, selective filling and inflation of the airholes in the PCF cladding are demonstrated. The technique may find important applications in tailoring or altering PCF characteristics and make it possible to seamlessly integrate various components/functions into PCFs.

Biointeraction analysis of carbamazepine binding to alpha1-acid glycoprotein by high-performance affinity chromatography.

Interactions of the drug carbamazepine with the serum protein alpha(1)-acid glycoprotein (AGP) were examined by high-performance affinity chromatography. Frontal analysis studies with an immobilized AGP column and control column indicated carbamazepine had both low-affinity interactions with the support and high-affinity interactions with AGP. When a correction was made for binding to the support, the association equilibrium constant measured at pH 7.

Entrapment of proteins in glycogen-capped and hydrazide-activated supports.

A method is described for the entrapment of proteins in hydrazide-activated supports using oxidized glycogen as a capping agent. This approach is demonstrated using human serum albumin (HSA) as a model binding agent. After optimization of this method, a protein content of 43 (+/-1)mg of HSA/g support was obtained for porous silica.

Immobilization of alpha1-acid glycoprotein for chromatographic studies of drug-protein binding II. correction for errors in association constant measurements.

A new method for the immobilization of alpha(1)-acid glycoprotein (AGP) in high-performance liquid chromatography (HPLC) columns was recently described for applications such as drug binding studies. Part of this earlier work used self-competition zonal elution studies to measure association equilibrium constants between immobilized AGP and R- or S-propranolol. It was later found that analysis of these data by a common equation derived for linear elution conditions gave erroneous values for experiments actually conducted under nonlinear conditions.

Development of an affinity silica monolith containing alpha1-acid glycoprotein for chiral separations.

An affinity monolith based on silica and containing immobilized alpha(1)-acid glycoprotein (AGP) was developed and evaluated in terms of its binding, efficiency and selectivity in chiral separations. The results were compared with data obtained for the same protein when used as a chiral stationary phase with HPLC-grade silica particles or monoliths based on a copolymer of glycidyl methacrylate (GMA) and ethylene dimethacrylate (EDMA). The surface coverage of AGP in the silica monolith was 18% higher than that obtained with silica particles and 61% higher than that measured for a GMA/EDMA monolith.

Evaluation of a hydrazide-linked alpha1-acid glycoprotein chiral stationary phase: separation of R- and S-propranolol.

The binding and chiral separation of R- and S-propranolol was investigated on a new type of alpha1-acid glycoprotein (AGP) column. This column was prepared through the controlled and mild oxidation of AGP, followed by the immobilization of this protein to hydrazide-activated silica. The effects of temperature, pH, ionic strength, and organic modifiers on the retention and separation of R- and S-propranolol were investigated on this column.

Immobilization of alpha(1)-acid glycoprotein for chromatographic studies of drug-protein binding.

A new method for preparing immobilized alpha1-acid glycoprotein (AGP) for use in drug-protein binding studies was developed and optimized. In this approach, periodate was used under mild conditions to oxidize the carbohydrate chains in AGP for attachment to a hydrazide-activated support. The final conditions chosen for this oxidation involved the reaction of 5.