The 1H NMR spectra were collected using a Varian MR400 spectrometer in deuterated chloroform solution with trimethylsilane (TMS) as reference. Gel permeation chromatography (GPC) spectra were collected on a Shimadzu GPC system with THF as the solvent. The samples used for NMR and GPC measurements were fabricated on quartz and encapsulated with a cover glass similar to the OPV device. The package lids were removed after light soaking under 1 sun illumination. Laser desorption/ionization time-of-flight mass spectra were collected using a Bruker AutoFlex Speed MALDI-TOF instrument from the aged thin-film sample under nitrogen laser pulse illumination.
Autoflex speed maldi tof instrument
Manufactured by Bruker
Sourced in Germany
The Autoflex Speed MALDI-TOF instrument is a mass spectrometry system designed for matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) analysis. It is capable of performing high-throughput, sensitive, and precise mass measurements of a wide range of biomolecules, including proteins, peptides, oligonucleotides, and other compounds.
Automatically generated - may contain errors
Lab products found in correlation
Gpc system, by Shimadzu (1 mentions)
400 mr spectrometer, by Agilent Technologies (1 mentions)
Fluorescent dye removal columns, by Thermo Fisher Scientific (1 mentions)
Pierce 660 nm protein assay, by Thermo Fisher Scientific (1 mentions)
Amicon ultra 0.5 ml centrifugal filter, by Merck Group (1 mentions)
8 protocols using autoflex speed maldi tof instrument
1
Characterization of Aged Organic Photovoltaic Thin Films
2
Profiling Salmonella Dublin Isolates from Cattle
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Salmonella Dublin diagnostic isolates from cattle (n = 140) were selected, 110 (78.5%) from clinical infections (n = 44 from lung, n = 34 from liver, n = 6 from intestine, n = 6 from feces, n = 20 from other sites) and 30 (21.4%) were of unknown clinical status, from 2014–2017 submissions for Salmonella serotyping archived at the NVSL. Samples came from 21 U.S. States (MN n = 37, IA n = 21, NY n = 17, SD n = 10, OH n = 7, IL n = 6, PA n = 6, TX n = 6, IN n = 5, WA n = 5, MO n = 5, KY n = 4, ID n = 2, WI n = 2, MD n = 1, AL n = 1, NE n = 1, KS n = 1, OK n = 1, MI n = 1, FL n = 1). Isolates details are available in S1 Table .
The dataset was initially limited to one sample per year per owner. If more than the targeted number of isolates remained, a randomly selected subset of isolates was chosen. The data were then de-identified to remove information other than the animal species, state of origin, clinical status, and sample type and assigned a unique identifier. Identity was confirmed using Biotyper software with an Autoflex Speed MALDI-TOF instrument (Bruker Daltonics).
The dataset was initially limited to one sample per year per owner. If more than the targeted number of isolates remained, a randomly selected subset of isolates was chosen. The data were then de-identified to remove information other than the animal species, state of origin, clinical status, and sample type and assigned a unique identifier. Identity was confirmed using Biotyper software with an Autoflex Speed MALDI-TOF instrument (Bruker Daltonics).
3
MALDI-TOF-MS Analysis of Seed Extracts
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Putative detection of peptides in the seed extract using MALDI-TOF-MS was prepared as previous study [25 (link)]. Triplicate 1 µL of the seed extracts (1 mg/mL) were spotted onto a MALDI plate (AnchorChip). After drying, 1 µL of MALDI matrix HCCA was added to each sample spot. The HCCA solution consisted of 10 mg of α-cyano-4-hydroxycinnamic acid dissolved in 70% (v/v) acetonitrile (ACN) containing 0.1% (v/v) trifluoroacetic acid (TFA). The spots were air dried so that the samples could co-crystallize with the matrix. Mass spectra profiles of the seed extracts were obtained using an Autoflex Speed MALDI-TOF instrument (Bruker, Germany) equipped with a Nd:YAG laser operating at 355 nm, a laser frequency of 50 Hz with 500 laser shots and an acceleration voltage of 20 kV. Data were collected between mass range of 1000 to 20,000 Da. Data from the plate was collected and analysed using the Flex Control software.
4
Sactipeptide Molecular Weight Analysis
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Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) was performed to determine the molecular weight (MW) of the purified sactipeptide using an Autoflex Speed MALDI-TOF instrument (Bruker, Germany). Matrix solution (10 mg of α-cyano-4-hydroxycinnamic acid dissolved in 70% acetonitrile containing 0.1% (v/v) trifluoroacetic acid), was mixed with an equal volume of the purified sactipeptide and 1 µl of the mixture was spotted onto the target plate, air dried and analysed. The molecular ion of mature sactipeptide was detected in the positive ion mode.
5
Mass Spectrometry of Intact Metalloprotein
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The mass of intact MtL was measured by mass spectrometry using an Autoflex Speed MALDI-TOF Instrument (BRUKER) calibrated with Bovine Serum Albumin (BSA) as molecular weight standard (M2+ 33216 Da, M+ 66431 Da, 2M+ 132861 Da). MtL was diluted in 0.1% tri-fluoro-acetic acid (TFA) to a final concentration of 20 μM, and mixed 1:1 with a saturated stock of α-cyano-4-hydroxycinnamic acid (α-CHCA) matrix in acetonitrile/TFA (33 v/v% / 0.1 v/v%).
6
Fluorescent Labeling of Interleukins
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A 100
μL portion of protein (1–2 mg/mL in PBS) was reacted
with 3 (IL-1β) or 6 (IL-1α) equiv of 5(6)-carboxy-X-rhodamine N-succinimidyl ester (15 mM in DMSO). Samples were incubated
for 1 h at room temperature while shaken at 1500 rpm on an Eppendorf
thermomixer. Excess of dye was removed using fluorescent dye removal
columns (Thermo Scientific) according to the manufacturer’s
instructions using Amicon Ultra 0.5 mL centrifugal filters (Millipore)
with a 100 kDa cutoff instead of the supplied spin columns. The protein
was eluted with PBS. The final concentration of the protein was determined
using the Pierce 660 nm protein assay (Thermo Fisher Scientific).
The degree of labeling was assessed by MALDI-TOF MS on a Bruker Autoflex
speed MALDI-TOF instrument. As for IL-1β, approximately 50%
monolabeled protein was obtained. IL-1α was labeled to a larger
extent, such that in addition to monolabeled protein, also difunctionalized
product was obtained (seeFigure S18 ).
μL portion of protein (1–2 mg/mL in PBS) was reacted
with 3 (IL-1β) or 6 (IL-1α) equiv of 5(6)-carboxy-X-rhodamine N-succinimidyl ester (15 mM in DMSO). Samples were incubated
for 1 h at room temperature while shaken at 1500 rpm on an Eppendorf
thermomixer. Excess of dye was removed using fluorescent dye removal
columns (Thermo Scientific) according to the manufacturer’s
instructions using Amicon Ultra 0.5 mL centrifugal filters (Millipore)
with a 100 kDa cutoff instead of the supplied spin columns. The protein
was eluted with PBS. The final concentration of the protein was determined
using the Pierce 660 nm protein assay (Thermo Fisher Scientific).
The degree of labeling was assessed by MALDI-TOF MS on a Bruker Autoflex
speed MALDI-TOF instrument. As for IL-1β, approximately 50%
monolabeled protein was obtained. IL-1α was labeled to a larger
extent, such that in addition to monolabeled protein, also difunctionalized
product was obtained (see
7
Comprehensive Salmonella Senftenberg Isolation
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A total of 94 S. Senftenberg isolates from swine (n = 50), poultry (n = 24) and cattle (n = 20) were selected from the National Veterinary Services Laboratories (NVSL) Salmonella repository isolates archived at room temperature on nutrient agar slants. Samples came from 20 US States (IA = 20, MN = 15, AR = 8, MO = 8, IL = 6, IN = 4, TX = 4, NC = 4, OH = 4, PA = 4, OK = 2, KS = 2, NE = 2, NY = 2, SD = 2, VA = 2, WI = 2, AL = 1, AZ = 1, KY = 1).
Isolates were selected from samples that were submitted to the NVSL for Salmonella serotyping, confirmed by classical (Grimont and Weill, 2007 ) and molecular typing using Luminex xMAP® technology (Dunbar et al., 2015 (link)), between the years of 2014 and 2017. The dataset was initially limited to one sample per year per owner. If more than the targeted number of isolates were available, a randomly selected subset of isolates was chosen. The data was then de-identified to remove information other than the animal species, state of origin, clinical status, and sample type and assigned a unique identifier. Salmonella was confirmed using Biotyper software with an autoflex speed™ MALDI-TOF instrument (Bruker Daltonics, Billerica, MA, USA).
Isolates were selected from samples that were submitted to the NVSL for Salmonella serotyping, confirmed by classical (Grimont and Weill, 2007 ) and molecular typing using Luminex xMAP® technology (Dunbar et al., 2015 (link)), between the years of 2014 and 2017. The dataset was initially limited to one sample per year per owner. If more than the targeted number of isolates were available, a randomly selected subset of isolates was chosen. The data was then de-identified to remove information other than the animal species, state of origin, clinical status, and sample type and assigned a unique identifier. Salmonella was confirmed using Biotyper software with an autoflex speed™ MALDI-TOF instrument (Bruker Daltonics, Billerica, MA, USA).
8
MALDI-TOF-MS analysis of bacteriocin
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The protein was subjected to matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) analyses as described by Vater et al. [48] . The MALDI-TOF mass spectra were recorded using an Autoflex Speed MALDI-TOF instrument (Bruker, Germany) containing a 355 nm Smartbeam II laser for desorption and ionization. 10 mg of αcyano-4-hydroxycinnamic acid dissolved in 70 % acetonitrile (ACN) containing 0.1 % (v/v) trifluoroacetic acid (TFA) was used as matrix solution. Five microliters of bacteriocin samples were mixed with equal volume of matrix solution and 1 µL of the mixture was spotted onto the target, air dried and measured.
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