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Biomedical subjects

F Körber

Publications and source records attributed to F Körber.

At least 19 recordsLinked to original sources

[Sonography of the optical nerve -- experience in 483 children].

INTRODUCTION: In case of increased intracranial pressure (IICP), the inflow of cerebrospinal fluid widens the space between the optic nerve (ON) itself and the surrounding dura mater leading to the sonographic appearance of increased diameter of the ON. The purpose of the study was to gain clinical experience in children and to determine (a) the mean values for patients without proven IICP and (b) pathologic values of those with proven IICP. MATERIALS AND METHODS: Ultrasound of the optic nerve was performed in 483 children with symptoms consistent with IICP, comprising 287 males and 196 females at an age ranging from 4 days to 24 years with a mean age of 7.5 + 5.1 years. The measured diameter of the ON of both eyes and the morphologic criteria concerning nerve sheath and papilla were evaluated retrospectively. RESULTS: Most of the investigated patients (n = 466) had no IICP as confirmed by neurological examination, EEG, sometimes CCT and/or MRI and clinical follow-up. The typical morphological findings in patients with normal intracranial pressure (ICP) were a clear and longitudinally extended demarcation of the ON with a well-delimited nerve sheath and without prominent papilla. The mean diameter of the ON in patients with normal ICP was 3.4 mm + 0.7 mm. In 17 patients with proven IICP, the mean diameter of the ON increased to 5.6 mm + 0.9 mm. Typically, the nerve sheath was indistinguishable from the hypoechoic ON, often but not invariably associated with a prominent papilla. In patients with IICP, the diameter of the ON alone matches the diameter of the ON plus nerve sheath in patients with normal ICP. CONCLUSION: IICP was detected with a high sensitivity by ultrasound using the diameter and the morphological criteria of an indistinguishable nerve sheath. A diameter of more than 4.5 mm is definitely pathologic and requires further investigation. Prominence of the papilla is an unreliable criterion for acute IICP.

Adolescent↗

Crystallization of two related lectins from the legume plant Dolichos biflorus.

The seed lectin DBL and the related stem and leaves lectin DB58 of the tropical legume Dolichos biflorus were crystallized, as well as complexes of DBL with adenine and with GalNAc(alpha1-3)[Fuc(alpha1-2)]Gal. The different crystal forms of DBL diffract to about 2.8 A, while DB58 crystals diffract to 3.3 A.

ABO Blood-Group System↗

Two crystal forms of the lentil lectin diffract to high resolution.

The legume lectins are an important class of polysaccharide-binding proteins with a wide range of biochemical and immunological applications. Two high-resolution crystal forms are obtained for the lentil (Lens culinaris) lectin: a monoclinic P21 and an orthorhombic P212121. The unit cell dimensions for the monoclinic form are a = 58.0 A, b = 56.0 A, c = 82.1 A, beta = 104.4 degrees, while for the orthorhombic form a = 56.4 A, b = 74.6 A, c = 124.9 A. The asymmetric unit contains one dimer in both cases. The crystals diffract to 1.7 A resolution using synchrotron radiation. Preliminary data have been collected to 2.3 A on both crystal forms using a conventional X-ray source.

Crystallography↗

Carrier membrane as a stationary phase for affinity chromatography and kinetic studies of membrane-bound enzymes.

The use of membrane supports as stationary phase, coupled with ligands of choice, allows all kinds of chromatography [Dj. Josić, K. Zeilinger, Y. Lim, M. Raps, W. Hofmann and W. Reutter, J. Chromatogr., 484 (1989) 327] and offers a powerful alternative to both soft gel chromatography and high-performance liquid chromatography. In this work we present affinity membrane chromatography for purification of the enzyme carbonic anhydrase from haemolysates of human erythrocytes. Furthermore, the coupling of the enzymes to the membrane support allows kinetic investigations. As an example, kinetic experiments were carried out by means of carbonic anhydrase coupled to the membrane support using 4-nitrophenyl acetate and 2-chloro-4-nitrophenyl acetate as substrates.

Carbonic Anhydrases↗

Purification of carbonic anhydrase isoenzymes by high-performance affinity chromatography and hydrophobic interaction chromatography.

Isoenzymes of carbonic anhydrase were purified by a combination of affinity chromatography and hydrophobic interaction chromatography. Immobilization of sulfonamides on an epoxy-activated support provided a stationary phase for affinity chromatography which was stable to hydrolysis by carbonic anhydrase. A first purification step allowed the isolation of enzymes directly from homogenates of human erythrocytes and rat stomach. Without any further preparation, except the addition of ammonium sulfate to the eluate from affinity chromatography, the isoenzymes could be separated by hydrophobic interaction chromatography with very high recovery of protein and retention of enzymatic activity.

Animals↗

Kinetic and inhibition studies of Bacillus cereus beta-lactamase using a spectrophotometric method.

The use of a spectrophotometric method is reported for the characterization of a beta-lactamase (EC 3.5.2.6) from Bacillus cereus. Absorption coefficients of the mercaptides of various penicillins were determined with this method. The enzyme was kinetically characterized using penicillins. Inhibition studies with Bacillus cereus beta-lactamase and various penicillins showed a substrate type of inhibition, indicating an additional binding site for substrates without catalytic activity. The dissociation constant of this binding site was determined and the influence of this binding site upon the catalytic activity is discussed. Studies with beta-lactamase-stable penicillins as inhibitors and various penicillins showed different types of inhibition, which indicated the presence of an additional catalytically inactive binding site. Experiments with clavulanic acid, a beta-lactamase inhibitor without remarkable intrinsic antibacterial activity, showed a mixed type of inhibition. Based on the hypothesis for the existence of more than one substrate binding site on the enzyme, clavulanic acid was found to be bonded to both the catalytic active and the catalytic inactive binding site.

Bacillus cereus↗