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Michael E. Bembenek

Researcher at University of Texas at Austin

Publications -  32
Citations -  1020

Michael E. Bembenek is an academic researcher from University of Texas at Austin. The author has contributed to research in topics: Engineering & Medicine. The author has an hindex of 5, co-authored 7 publications receiving 899 citations. Previous affiliations of Michael E. Bembenek include Johns Hopkins University School of Medicine & Nemours Foundation.

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cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties.

TL;DR: Using oligonucleotide probes derived from three sequenced peptide fragments, isolated cDNA clones that encode the A and B forms of monoamine oxidase are isolated and the nucleotide sequences of these cDNAs are determined.
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Identification and purification of diphosphoinositol pentakisphosphate kinase, which synthesizes the inositol pyrophosphate bis(diphospho)inositol tetrakisphosphate

TL;DR: This work reports the identification and purification of another novel kinase, diphosphoinositol pentakisphosphate (PP-IP5) Kinase, which uses PP- IP5 as a substrate to form bis(diphospho)inositol tetrakisphosphates (bis- PP-IP4) in soluble fractions of rat forebrain.
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Microstructure and Wear Characterization of the Fe-Mo-B-C—Based Hardfacing Alloys Deposited by Flux-Cored Arc Welding

TL;DR: In this paper , an analysis of common reinforcement methods of machine parts and theoretical bases for the selection of their chemical composition were carried out, including the development of the chemical composition of tungsten-free hardfacing alloys based on the Fe-Mo-B-C system and hardfacing technology and the investigation of the microstructure and the mechanical properties of the developed hardface alloys.
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Mammalian Alkaloids: O‐methylation of (S)‐ and (R)‐dideoxynorlaudanosoline‐1‐carboxylic acid by catechol O‐methyltransferase and identification of a yellow pigment obtained at physiological pH

TL;DR: The structure of quinonemethide 4A was determined on the basis of spectral data, by its conversion into isoquinolines of established structure, and by synthesis, and was found to be a weak inhibitor of monoamine oxidase A (MAO A) but not a substrate.