Abigail M. Tokheim

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Using antiserum against the recombinant isoform 3 of mouse brain metallothionein (MT3), the amount of MT3 protein was determined in whole brain homogenates from the Tg2576 transgenic mouse model of Alzheimer's Disease. Twenty-two month old transgenic positive mice showed a 27% decrease of MT3 normalized to the total protein in the extracts compared to same(More)
Using mouse hearts from Swiss Webster mice, calcineurin was immunoprecipitated using commercially available anti-calcineurin antibody and the resulting complex analyzed by using sodium dodecyl sulfate-gel electrophoresis with silver staining. Distinct proteins were observed and subjected to in situ trypsin digestion followed by extraction of the resulting(More)
Using immunological approaches and mass spectrometry, five proteins associated with metallothionein-3 in mouse brains have been identified. Metallothionein-3 and associated proteins were isolated using immunoaffinity chromatography over immobilized anti-mouse brain MT3 antibody. Proteins in the recovered pool were separated by SDS-polyacrylamide gel(More)
The Homology module within Insight-II was used to model residues 374-420, sequences missing in the coordinates of resolved structure of the catalytic subunit of calcineurin. The modeling was done in two segments. The calmodulin binding region from residues 389 to 420 was modeled based on the structure of two other proteins having calmodulin binding domains(More)
The recombinant form of isoform-3 of mouse brain metallothionein (MT3) was used as an antigen to immunize rabbits and raise MT3-selective antiserum. The antiserum was essentially specific for MT3 with 100-fold greater sensitivity for MT3 compared to MT1 or MT2. Immunonblot analysis of whole mouse brain homogenates showed that MT3 was present only in the(More)
From earlier studies on calcineurin, the presence of multiple double bonds in putative inhibitors was hypothesized as critical features for effective inhibition. Polyunsaturated fatty acids were tested as inhibitors of calcineurin and found to inhibit the phosphatase activity of calcineurin although effective inhibition was observed only in the absence of(More)
Often used to remove sulfate groups from carbohydrates, the regulatory properties of the aryl sulfatase from Helix pomatia remain little characterized. As many hydrolytic enzymes utilize exogenous metal ions in catalysis, the effect of various divalent metal ions on the sulfatase was investigated. Evidence for metal ion activation was collected, with Cd2+(More)
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