Publications by authors named "Donna J Spannaus-Martin"

Over the past five years our clinical laboratory sciences (CLS) program more than doubled student enrollment to help address the workforce shortages in our state. At the same time, medical laboratory technician programs were also increasing enrollment, putting significant pressure on the already limited number of clinical training spaces. To help alleviate the impact on clinical sites, major changes were made to the traditional clinical rotation model; shifting from a clinical training to a clinical experience and a simultaneous decrease in length from 22 to 12 weeks.

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Objective: To evaluate the 2007 and 1990 data on the number and characteristics of programs offering graduate level degrees in Clinical Laboratory Science. DESIGN/SETTING/PARTICIPANT: Data were collected from published sources (Directory of Graduate Programs for Clinical Laboratory Practitioners) and analyzed at the University of Minnesota. Specific data regarding the kinds of advanced programs and the number of graduates per year, the number of program openings and closures, program requirements were collected, as well as data regarding the number and employment of graduates of Master's degree programs at two long-standing public institutions.

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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 with the same 1-8-14 structural motif as calcineurin.

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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 Cd(2+) being notable for effective activation.

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para-Nitrophenyl phosphorothioate (pNPT) was hydrolyzed by calcineurin at initial rates slightly, but comparable to rates for para-nitrophenyl phosphate (pNPP). Kinetic characterization yielded higher estimates for both Km and Vmax compared to pNPP. Metal ion activation of phosphorothioate hydrolysis was more promiscuous.

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Recombinant calcineurin heterodimer with the full length delta-isoform of the catalytic subunit (CaN(500)) was expressed in insect cells using the baculovirus system and compared to native bovine brain enzyme in its response to divalent metal ions, redox reagents, and enzymatic modification of arginine residues. The response to various metal ions showed essentially the same profile as bovine brain calcineurin, although Co2+ and Zn2+ did not support recombinant activity as well. Kinetic analysis showed that metal ion and substrate binding were not independent, as found for the bovine brain calcineurin.

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