Albert N. Nelson
Mayo Clinic
15 Papers
156 Citations
Albert N. Nelson is an academic researcher from Mayo Clinic. The author has contributed to research in topics: Aldehyde dehydrogenase & Histamine H1 receptor. The author has an hindex of 9, co-authored 15 publications.
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Papers
Antagonism by neuroleptics of neurotransmitter receptors of normal human brain in vitro.
TL;DR: Using radioligand binding techniques, the equilibrium dissociation constants (KD's) for a series of neuroleptics at the dopamine, muscarinic, histamine H1, alpha 1- and alpha 2-adrenergic receptors of normal human brain tissue obtained at autopsy were determined.
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A comparison of procedures for attaching steroidal glucosiduronic acids to bovine serum albumin.
TL;DR: Steroidal glucosiduronic acids can be joined to bovine serum albumin under mild conditions by use of either N-hydroxysuccinimide or isobutyl chloroformate, the more efficient of the two coupling agents.
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Reduced D2 dopamine and muscarinic cholinergic receptor densities in caudate specimens from fluctuating parkinsonian patients.
J. Eric Ahlskog,Elliott Richelson,Albert N. Nelson,Patrick J. Kelly,Haruo Okazaki,Gertrude M. Tyce,Jon A. van Heerden,Susan L. Stoddard,Stephen W. Carmichael +8 more
TL;DR: Receptor deficits could have been a reflection of more widespread degenerative cerebral disease, although levodopa‐refractory symptoms were generally not pronounced in these patients.
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[3H]neurotensin(8-13) binds in human brain to the same sites as does [3H]neurotensin but with higher affinity
TL;DR: The results suggest that [3H]neurotensin(8–13) binds to the same sites as [3F]‐neuroTensin and that [2H]‐NeurotENSin has a higher affinity for these sites in human brain than [3G]‐NEurotensein, which has been suggested to have a lower affinity.
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S-methyl-N,N-diethylthiocarbamate sulfoxide and S-methyl-N,N-diethylthiocarbamate sulfone, two candidates for the active metabolite of disulfiram
TL;DR: The results suggest that MeDTC sulfone is highly reactive with normal cellular constituents (e.g., glutathione), which may protect ALDH from inhibition, unless this inhibitor is formed very near the target enzyme.
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