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T Lederer

Publications and source records attributed to T Lederer.

25 records · Page 2Linked to original sources
PubMed1992

An accurate method for determining the helical repeat of DNA in solution reveals differences to the crystal structures of two B-DNA decamers.

Many DNA sequences have been studied by X-ray crystallography with the goal of deciphering a sequence-structure code. We have determined the helical repeats of two B-type DNA decamers in solution employing an electrophoretic method based on phasing of bent segments. The decamers contain recognition sites for the dcm methyltransferase and for the restriction nuclease NarI with a mutational hotspot. Their helical repeats are 10.59(+/- 0.05) bp and 10.52(+/- 0.03) bp, respectively, whereas crystallographic analysis yielded 10.0 bp in the solid state. This difference is greater than that for the transition between B- and A-type DNA in solution. Thus, reliable information about the polymorphism of DNA in solution must be based on both X-ray and solution data. We describe a generally applicable approach to accurately determine helical repeats of small DNA duplexes in solution.

Base Sequence↗
PubMed1991

Revised radioreceptor assay for beta 2-adrenoceptors expressed on peripheral mononuclear leukocytes.

Peripheral mononuclear leukocytes (pMNL) bear a population of beta 2-adrenoceptors. Radioreceptor assays with (-)-125Iodocyanopindolol (125I-CYP) are often used to determine the expression of these hormone receptors under physiological and pathological conditions. Doubts on the occurrence of just one class of binding sites as well as the availability of new laboratory equipment prompted us to revise the procedure employed for investigation of these receptors. pMNL were harvested from venous human blood by density centrifugation with LymphopaqueR, LymphoprepR, or FicollR yielding immunologically distinct pMNL fractions. Receptor binding assays were performed semi-automatically with 125I-CYP in the range from 0.6-600 pmol/l. Analysis of the data (modified affinity spectra, Scatchard plot) revealed two classes of binding sites (high- and low affinity binding). The binding isotherms were sigmoidal in the concentration range from 0.6-3.0 pmol/l. Parameters estimated for the high affinity binding site may vary by a factor of 10, depending on the mathematical model employed.

Humans↗
PubMed1975

The effect of parenteral alimentation fluid, undiluted with saline or fresh sera, on the growth of Candida albicans in vitro at 37 degrees C.

Parenteral alimentation is often complicated by Candida albicans infection which may be fatal. This study investigated the effect of alimentation fluid (Aminosol) on C. albicans' growth in vitro. It was found that concentrated Aminosol (1400 millisomoles) maintained C. albicans in a viable state but inhibited replication. Dilution of alimentation fluid to physiological concentrations (300 milliosmoles) with either saline or aged pooled normal sera promoted in vitro growth of C. albicans which was equivalent to that obtained in BHI broth and was slightly less than that obtained in Sabouraud's broth. The effects of fresh sera with full complement activity were also investigated. In fresh sera appropriately diluted with physiological saline, some clumping of the yeasts was observed and all formed germ tubes. Growth as defined by budding or the formation of hyphae was inhibited. When Aminosol was diluted to 300 milliosomoles with fresh sera, all yeasts were noted to be in clumps with germ tubes as well as continually growing hyphae. Growth was approximately equal to that seen in Aminosol similarly diluted with saline.

Blood Proteins↗