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D L Weller

Publications and source records attributed to D L Weller.

16 recordsLinked to original sources
PubMed1996

Resistance of morpholino phosphorodiamidate oligomers to enzymatic degradation.

Oligomers possessing the Morpholino phosphorodiamidate backbone were evaluated for resistance to a variety of enzymes and biologic fluids. A 25-mer was incubated with nucleases, proteases, esterases, and serum, and the reaction mixtures were directly analyzed by MALDI-TOF mass spectrometry. The 25-mer was completely resistant to 13 different hydrolases and serum and plasma. The excellent resistance of Morpholino phosphorodiamidates to enzymatic attack indicates their suitability for in vivo use.

Blood Physiological Phenomena↗
PubMed1983

Preliminary characterization of ribosomes of Entamoeba invadens.

The ribosomes of Entamoeba invadens trophozoites have sedimentation coefficients of 77, 53 and 36 S. Most of the ribosomal proteins are basic and their one- and two-dimensional electrophoretic patterns differ from the corresponding patterns of Escherichia coli and Saccharomyces cerevisiae. Two dozen bands were observed in the 10 000 to 100 000 molecular weight range following sodium dodecylsulfate-gel electrophoresis of amoebal ribosomal proteins. Long, thin pronase-sensitive structures were seen in electron micrographs of E. invadens ribosomal preparations.

Animals↗
PubMed1981

Ribonuclease of Entamoeba invadens.

Two bands of RNAase activity were observed on gel electrophoresis of fractions obtained during partial purification of the RNAase of Entamoeba invadens. The faster migrating band which was responsible for most of the RNAase activity was isolated by gel electrophoresis. A pI of 5.5 was determined for this RNAase activity and estimates of its molecular weight and sedimentation coefficient gave values of about 25 000 and approximately 2.8 S. It exhibited maximum activity around pH 6, and digestion of RNA showed a pattern expected of an endoribonuclease.

Animals↗
PubMed1981

A simple procedure for partial purification of an RNAase of Entamoeba invadens.

The behavior of an RNAase, present in centrifugally clarified homogenates of axenic trophozoites of Entamoeba invadens, on isoelectric focusing (IEF) and agarose-poly(G) chromatography is described. The results led to a simple two-step procedure for partial purification of the RNAase in which fractionation of the homogenate by IEF is followed by agarose-poly(G) chromatography. Recovery of enzyme activity has ranged from 50 to 80% of that present in homogenates, and increases of 80- to 160-fold in the specific activity have been obtained using the procedure. A single zone of activity was observed on analysis of the partially purified RNAase by sucrose gradient IEF and velocity zonal ultracentrifugation.

Animals↗