E
Ernest V. Groman
Researcher at Harvard University
Publications - 5
Citations - 182
Ernest V. Groman is an academic researcher from Harvard University. The author has contributed to research in topics: Cofactor & Dehydrogenase. The author has an hindex of 5, co-authored 5 publications receiving 181 citations. Previous affiliations of Ernest V. Groman include MetroHealth.
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Journal Article
Ferrite particles: a new magnetic resonance imaging contrast agent. Lack of acute or chronic hepatotoxicity after intravenous administration.
Bruce R. Bacon,Bruce R. Bacon,David D. Stark,David D. Stark,Chanho H. Park,Chanho H. Park,Sanjay Saini,Sanjay Saini,Ernest V. Groman,Ernest V. Groman,Peter F. Hahn,Peter F. Hahn,Carolyn C. Compton,Carolyn C. Compton,Joseph T. Ferrucci,Joseph T. Ferrucci +15 more
TL;DR: Quantitative iron determinations and microscopic studies suggest that ferrite particles may be partially degraded and that iron is cleared from the liver during a 3-month period, as well as finding no evidence of iron-induced hepatocellular injury.
Book ChapterDOI
Human placental 17beta-estradiol dehydrogenase: characterization and structural studies.
Lewis L. Engel,Ernest V. Groman +1 more
TL;DR: It has been found that human term placenta is very rich in an enzyme that oxidizes estradiol to estrone and a 50-fold purification of this enzyme is named 17β-estradiol dehydrogenase.
Journal ArticleDOI
Hydroxysteroid dehydrogenases of Pseudomonas testosteroni. Separation of a 17 beta-hydroxysteroid dehydrogenase from the 3(17) beta-hydroxysteroid dehydrogenase and comparison of the two enzymes.
Ernest V. Groman,Lewis L. Engel +1 more
TL;DR: A protein fraction containing the enzyme corresponding to the fastest migrating band and devoid of the other hydroxysteroid dehydrogenase activities has been obtained, and appears to be distinct from the previously isolated 3(17) beta-hydroxysteroid dehydration.
Book ChapterDOI
Catalytic competence: a direct criterion for affinity labeling.
TL;DR: This chapter examines and provides evidence that the reaction of potential affinity label, 3-bromoacetoxyestrone, with human placental estradiol dehydrogenase and finds that it satisfies the first four criteria for an affinity label.
Journal ArticleDOI
Horse‐Liver Alcohol Dehydrogenase and Pseudomonas testosteroni 3(17)β‐Hydroxysteroid Dehydrogenase Transfer Epimeric Hydrogens from NADH to 17β‐Hydroxy‐5α‐androstan‐3‐one
TL;DR: Observations provide an exception to the rule proposed by Alworth and Bentley that with regard to the paired methylene hydrogens at C-4 of NADH and NADPH "the stereospecificity of a particular reaction is fixed and does not vary with the source of the enzyme preparation".