Biomedical subjects

K Kauffmann

Publications and source records attributed to K Kauffmann.

3 recordsLinked to original sources

PubMed1998

Beta-trace protein concentration in cerebrospinal fluid is decreased in patients with bacterial meningitis.

Although meninges represent a major site of biosynthesis, beta-trace protein (beta-trace) has not been studied in the cerebrospinal fluid (CSF) of meningitis patients. We measured beta-trace in lumbar CSF of normal controls (n = 27) and in patients with various neurological diseases (n = 92) by an immunonephelometric assay. The mean concentration of beta-trace in CSF of control patients was 16.6+/-3.6 mg/l. In bacterial meningitis (n = 41), CSF beta-trace was significantly decreased (8.7+/-3.9 mg/l; P< 0.001), whereas in spinal canal stenosis it was elevated (29.2+/-10.3 mg/l; P= 0.002). In viral meningoencephalitis (n = 12), beta-trace CSF concentrations were normal. Beta-trace concentrations remained below the normal range even after curing of bacterial meningitis, and normalisation of CSF leucocytes and blood-CSF barrier function. Beta-trace may be a useful tool for studying the pathophysiology of bacterial meningitis.

Adult↗

PubMed1997

An Fe2IVO2 diamond core structure for the key intermediate Q of methane monooxygenase.

A new paradigm for oxygen activation is required for enzymes such as methane monooxygenase (MMO), for which catalysis depends on a nonheme diiron center instead of the more familiar Fe-porphyrin cofactor. On the basis of precedents from synthetic diiron complexes, a high-valent Fe2(micro-O)2 diamond core has been proposed as the key oxidizing species for MMO and other nonheme diiron enzymes such as ribonucleotide reductase and fatty acid desaturase. The presence of a single short Fe-O bond (1.77 angstroms) per Fe atom and an Fe-Fe distance of 2.46 angstroms in MMO reaction intermediate Q, obtained from extended x-ray absorption fine structure and Mössbauer analysis, provides spectroscopic evidence that the diiron center in Q has an Fe2IVO2 diamond core.

Binding Sites↗

PubMedDate not supplied

Selection effects on a linked neutral locus.

Selection changes the frequency of alleles at a linked locus as well as at those under selection if the population is not in linkage equilibrium. The magnitude of this frequency change depends on the tightness of the linkage, the selection intensity, and the deviation from linkage equilibrium. Allowing a population to mate randomly without selection brings the population closer to linkage equilibrium. This decreases the effect of selection on allelic frequencies at a linked neutral locus. However, if linkage is very tight it can take many generations to make a large difference in the effect of the linked locus. The loss due to undesirable changes in allelic frequencies at linked loci when the population is not in linkage equilibrium must be weighed against the time and effort saved by beginning intense selection for the primary trait in an early generation. Effects of selection intensity, linkage intensity, and delayed selection on changes in allelic frequency at a neutral linked locus are demonstrated.

Alleles↗