Characterization of butyrylcholinesterase from porcine milk.

Ashima Saxena, Tatyana Belinskaya, Lawrence M Schopfer, Oksana Lockridge

Open access · hybridAbstract read

In one paragraph

Article in Archives of biochemistry and biophysics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it

0cells of the map it votes in

3citing papers in PubMed

1.7field-weighted citation impact, top 17% of its field

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 15 citations in OpenAlex.

Polyproline-rich peptides associated with Torpedo californica acetylcholinesterase tetramers.Chemico-biological interactions · 2020
Article
Purification of recombinant human butyrylcholinesterase on Hupresin®.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2018
Article
Tetramer organizing polyproline-rich peptides identified by mass spectrometry after release of the peptides from Hupresin-purified butyrylcholinesterase tetramers isolated from milk of domestic pig (Data in brief · 2018
Article

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Ashima SaxenaDivision of Biochemistry, Walter Reed Army Institute of Research, 503 Robert Grant Avenue, Silver Spring, MD 20910-7500, USA. Electronic address: ashima.saxena.civ@mail.mil.

Tatyana BelinskayaDivision of Biochemistry, Walter Reed Army Institute of Research, 503 Robert Grant Avenue, Silver Spring, MD 20910-7500, USA; Infectious Diseases Research Directorate, Naval Medical Research Center, 503 Robert Grant Avenue, Silver Spring, MD 20910-7500, USA. Electronic address: tatyana.belinskaya.ctr@med.navy.mil.

Lawrence M SchopferEppley Institute, University of Nebraska Medical Center, Omaha, NE 68198, USA. Electronic address: lmschopf@unmc.edu.

Oksana LockridgeEppley Institute, University of Nebraska Medical Center, Omaha, NE 68198, USA. Electronic address: olockrid@unmc.edu.

University of Nebraska Medical Center · USWalter Reed Army Institute of Research · US

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Joann B. Sweasy · 1985 to 2026

$55.0M

NCI NIH HHS P30 CA036727

6 · The paper itself

Abstract

Human butyrylcholinesterase (HuBChE) is under development for use as a pretreatment antidote against nerve agent toxicity. Animals are used to evaluate the efficacy of HuBChE for protection against organophosphorus nerve agents. Pharmacokinetic studies of HuBChE in minipigs showed a mean residence time of 267 h, similar to the half-life of HuBChE in humans, suggesting a high degree of similarity between BChE from 2 sources. Our aim was to compare the biochemical properties of PoBChE purified from porcine milk to HuBChE purified from human plasma. PoBChE hydrolyzed acetylthiocholine slightly faster than butyrylthiocholine, but was sensitive to BChE-specific inhibitors. PoBChE was 50-fold less sensitive to inhibition by DFP than HuBChE and 5-fold slower to reactivate in the presence of 2-PAM. The amino acid sequence of PoBChE determined by liquid chromatography tandem mass spectrometry was 91% identical to HuBChE. Monoclonal antibodies 11D8, mAb2, and 3E8 (HAH 002) recognized both PoBChE and HuBChE. Assembly of 4 identical subunits into tetramers occurred by noncovalent interaction with polyproline-rich peptides in PoBChE as well as in HuBChE, though the set of polyproline-rich peptides in milk-derived PoBChE was different from the set in plasma-derived HuBChE tetramers. It was concluded that the esterase isolated from porcine milk is PoBChE.

Indexed as

AcetylthiocholineAmino Acid SequenceAnimalsButyrylcholinesteraseButyrylthiocholineChromatography, LiquidHumansMilkPeptidesSubstrate SpecificitySwineSwine, MiniatureTandem Mass SpectrometryAcetylthiocholineButyrylcholinesteraseButyrylthiocholinePeptidespolyprolineAcetylcholinesteraseButyrylcholinesteraseHupresinPolyprolinePorcineTetramer

Identifiers

PMID29908755

DOI10.1016/j.abb.2018.06.006

PMCPMC6086383

OpenAlexW2807777635

What OpenQuestion holds

Textmetadata

LicenceTDM

Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.