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Equine myoglobin

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Equine myoglobin is a protein found in the muscle tissue of horses. It is responsible for the storage and transport of oxygen within the muscle cells. Myoglobin is a useful tool in laboratory settings for research and analysis.

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Lab products found in correlation

Bovine ubiquitin, by Merck Group (3 mentions) Bovine serum albumin (bsa), by Merck Group (3 mentions) Equine cytochrome c, by Merck Group (2 mentions) Human hemoglobin, by Merck Group (2 mentions) Bovine cytochrome c, by Merck Group (1 mentions) Ammonium acetate, by Thermo Fisher Scientific (1 mentions) Micro bio spin 6, by Bio-Rad (1 mentions) Methanol, by Merck Group (1 mentions) Acetic acid, by Fujifilm (1 mentions) Ammonium acetate, by Fujifilm (1 mentions) Methanol, by Fujifilm (1 mentions) Milli q advantage a10, by Merck Group (1 mentions) Bovine carbonic anhydrase, by Merck Group (1 mentions) Formic acid, by Thermo Fisher Scientific (1 mentions) Methanol, by Thermo Fisher Scientific (1 mentions) Optima lc ms grade water, by Thermo Fisher Scientific (1 mentions) Porcine hemin, by Merck Group (1 mentions) 48 well microtiter plate, by Thermo Fisher Scientific (1 mentions) Tryptic soy broth (tsb), by Thermo Fisher Scientific (1 mentions) Alcohol dehydrogenase, by Merck Group (1 mentions)

14 protocols using equine myoglobin

1

Protein Sample Preparation and Characterization

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Methanol (> 99.9% purity) was purchased from Sigma-Aldrich (UK). Ammonium acetate was supplied by Fisher Scientific (Loughborough, UK). Ultrapure water was obtained from a Milli-Q Advantage A10 ultrapure water filtration system (Merck Millipore, Darmstadt, Germany).
Bovine ubiquitin, equine myoglobin and bovine cytochrome c were purchased from Sigma-Aldrich (UK) as lyophilized powders with purities of ≥ 98, 90 and 95% respectively. Proteins were dissolved in 200 mM Ammonium acetate. Myoglobin in Ammonium acetate was desalted twice using Micro Bio-Spin 6 chromatography columns (Bio-Rad Laboratories, Hercules, CA, US).
All samples were diluted to a final protein concentration of 10 μM.
Theisen A., Black R., Corinti D., Brown J.M., Bellina B, & Barran P.E. (2018). Initial Protein Unfolding Events in Ubiquitin, Cytochrome c and Myoglobin Are Revealed with the Use of 213 nm UVPD Coupled to IM-MS. Journal of the American Society for Mass Spectrometry, 30(1), 24-33.
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2

Myoglobin-based Beef Patty Replica

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Example 29

In one example, a cold-set gel comprising myoglobin was prepared by first heat denaturing a 6% (w/v) solution of pea-vicilins in 20 mM potassium phosphate buffer, pH 7.4 with 100 mM sodium chloride at 100° C. for 30 minutes. The solution was allowed to cool back to room temperature. Canola oil (from Jedwards International) and equine myoglobin (Sigma) were added to a final concentration of 20% (v/v) and 1% (w/v), respectively. Gel formation was induced by adding calcium chloride at 20 mM. A 50 g beef patty replica was formed by combining 5 g of the cold gel with 10 g of adipose tissue-replica, 10 g of connective tissue-replica, and 25 g of muscle tissue-replica. Five mls of a 7% (w/w) solution of crude lentil protein was added to the mixture and patties were formed.

US10993462B2. Methods and compositions for consumables (2021-05-04). Impossible Foods Inc. [US]. Inventors: Marija Vrljic [US], Sergey Solomatin [US], Rachel Fraser [US], Patrick O'Reilly Brown [US], Jessica Karr [US], Celeste Holz-Schietinger [US], Michael Eisen [US], Ranjani Varadan [US].
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3

Cold-Set Gel Beef Patty Replica

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Example 29

In one example, a cold-set gel comprising myoglobin was prepared by first heat denaturing a 6% (w/v) solution of pea-vicilins in 20 mM potassium phosphate buffer, pH 7.4 with 100 mM sodium chloride at 100° C. for 30 minutes. The solution was allowed to cool back to room temperature. Canola oil (from Jedwards International) and equine myoglobin (Sigma) were added to a final concentration of 20% (v/v) and 1% (w/v), respectively. Gel formation was induced by adding calcium chloride at 20 mM. A 50 g beef patty replica was formed by combining 5 g of the cold gel with 10 g of adipose tissue-replica, 10 g of connective tissue-replica, and 25 g of muscle tissue-replica. Five mls of a 7% (w/w) solution of crude lentil protein was added to the mixture and patties were formed.

US11013250B2. Methods and compositions for consumables (2021-05-25). Impossible Foods Inc. [US]. Inventors: Marija Vrljic [US], Sergey Solomatin [US], Rachel Fraser [US], Patrick O'Reilly Brown [US], Jessica Karr [US], Celeste Holz-Schietinger [US], Michael Eisen [US], Ranjani Varadan [US].
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4

Calibration of Ion Mobility Measurements

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CA2 from bovine erythrocytes was purchased from Sigma (St. Louis, MO). Equine myoglobin and equine cytochrome c, which were used as calibrants for CCS measurements, were obtained from Sigma. All other reagents, such as acetic acid, ammonium acetate, and methanol were of the highest grade available and obtained from Wako Pure Chemical Industries, Ltd. (Osaka, Japan). Purified water was prepared by Milli-Q Advantage A10 (Merck Millipore, Billerica, MA).
Nabuchi Y., Hirose K, & Takayama M. (2018). pH Dependence of the Number of Discrete Conformers of Carbonic Anhydrase 2, as Evaluated from Collision Cross-Section Using Ion Mobility Coupled with Electrospray Ionization. Mass Spectrometry, 7(1), A0064.
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5

Protein Preparation for Native and Denaturing MS

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Bovine carbonic anhydrase,
equine myoglobin, and bovine ubiquitin were purchased as solids from
Sigma-Aldrich. Streptavidin was purchased as a solid from Pierce.
The trastuzumab heavy chain T12 peptides containing position 4 aspartic
acid isomers were purchased from Biomatik. For denaturing analysis,
carbonic anhydrase and ubiquitin were reconstituted to final concentrations
of 10 and 1 μM, respectively, in 50:50 water/acetonitrile with
0.1% formic acid. The trastuzumab peptides were mixed in a 1:1 ratio
at a total peptide concentration of 1 μM in 0.1% formic acid
in water. For native MS analysis, carbonic anhydrase, myoglobin, and
streptavidin were reconstituted to final concentrations of 5 μM
in 200 mM ammonium acetate. Carbonic anhydrase and streptavidin were
subsequently buffer-exchanged against 200 mM ammonium acetate using
Bio-Rad MicroBioSpin 6 gel filtration spin columns for further sample
cleanup.
Shaw J.B., Cooper-Shepherd D.A., Hewitt D., Wildgoose J.L., Beckman J.S., Langridge J.I, & Voinov V.G. (2022). Enhanced Top-Down Protein Characterization with Electron Capture Dissociation and Cyclic Ion Mobility Spectrometry. Analytical Chemistry, 94(9), 3888-3896.
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6

Protein Standards Characterization by MS

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The protein standards bovine ubiquitin (8.5 kDa), equine cytochrome c (12.3 kDa), equine myoglobin (Mb, 17.5 kDa), human hemoglobin (Hb, 64.4 kDa) and bovine serum albumin (BSA, 66.4 kDa) as well as MS grade salt ammonium acetate were purchased from Sigma-Aldrich (Gillingham, UK). Optima™ LC/MS grade water, methanol, and formic acid were obtained from Fisher Scientific (Loughborough, UK). A solution containing each protein at 50 μM was prepared in three conditions: 1) water; 2) 200 mM ammonium acetate and 3) 1:1 water/methanol (v:v) with 0.1% formic acid. Ten-microliter aliquots of each protein solution were spotted onto plain glass microscope slides and left to air dry.
Yan B, & Bunch J. (2021). Probing Folded Proteins and Intact Protein Complexes by Desorption Electrospray Ionization Mass Spectrometry. Journal of the American Society for Mass Spectrometry, 32(3).
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7

Pea Protein-based Meat Replica

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Example 29

In one example, a cold-set gel comprising myoglobin was prepared by first heat denaturing a 6% (w/v) solution of pea-vicilins in 20 mM potassium phosphate buffer, pH 7.4 with 100 mM sodium chloride at 100° C. for 30 minutes. The solution was allowed to cool back to room temperature. Canola oil (from Jedwards International) and equine myoglobin (Sigma) were added to a final concentration of 20% (v/v) and 1% (w/v), respectively. Gel formation was induced by adding calcium chloride at 20 mM. A 50 g beef patty replica was formed by combining 5 g of the cold gel with 10 g of adipose tissue-replica, 10 g of connective tissue-replica, and 25 g of muscle tissue-replica. Five mls of a 7% (w/w) solution of crude lentil protein was added to the mixture and patties were formed.

US10039306B2. Methods and compositions for consumables (2018-08-07). Impossible Foods Inc. [US]. Inventors: Marija Vrljic [US], sergey Solomatin [US], Rachel Fraser [US], Patrick O'Reilly Brown [US], Jessica Karr [US], Celeste Holz-Schietinger [US], Michael Eisen [US], Ranjani Varadan [US].
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8

Protein Sample Preparation Protocol

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Unless otherwise indicated, all reagents and solvents were obtained from commercial suppliers (Sigma and Fisher) and used without further purification. Protein samples of BSA and equine myoglobin were purchased from Sigma. ApoMb was prepared from equine myoglobin (Sigma) as per a modified protocol of Breslow (1965)46 (link) and Adams (1977)47 (link) outlined in supplementary information.
Dorh N., Zhu S., Dhungana K.B., Pati R., Luo F.T., Liu H, & Tiwari A. (2015). BODIPY-Based Fluorescent Probes for Sensing Protein Surface-Hydrophobicity. Scientific Reports, 5, 18337.
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9

Bacterial Growth in Iron-Limited Conditions

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All bacterial strains generated and/or used in this study are listed in Key resources table. For growth in iron limited conditions, bacteria were grown overnight in Tryptic Soy Broth (TSB) (Oxoid). Cells were harvested by centrifugation, washed with RPMI containing 10 µM EDDHA (LGC standards), adjusted to an OD600 = 1 and 2,5 µl were used to inoculate 0,5 ml of RPMI+ 1% casamino acids (BACTO) + 10 µM EDDHA in individual wells of a 48 well microtiter plate (NUNC). As sole iron source 200 nM porcine hemin (Sigma), 2.5 µg/ml human hemoglobin (own preparation), 10 µg/ml human myoglobin (Sigma) or equine myoglobin (Sigma), 117 nM human haptoglobin-hemoglobin or 200 nM hemopexin-heme (Sigma) were added to the wells. Bacterial growth was monitored using an Epoch2 reader (300 rpm, 37°C). The OD600 was measured every 15 min.
Jochim A., Adolf L., Belikova D., Schilling N.A., Setyawati I., Chin D., Meyers S., Verhamme P., Heinrichs D.E., Slotboom D.J, & Heilbronner S. (2020). An ECF-type transporter scavenges heme to overcome iron-limitation in Staphylococcus lugdunensis. eLife, 9, e57322.
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10

Analyzing Enzyme Quaternary Structure

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The quaternary forms of the enzymes were analyzed by non-denaturating gel electrophoresis and gel filtration methods. The gel electrophoresis was carried out by using pore-limited gradient polyacrylamide (4%–30%) [13 (link)]. Gel filtration was carried out on an accurate Sephacryl S-200 (Sigma-Aldrich, Schnelldorf, Germany) column equilibrated by mobile phase buffer consisting of 20 mM Tris-HCI pH 8.0 and 100 mM NaCI. The reference proteins ferritin (440 kDa), amylase (200 kDa), alcohol dehydrogenase (150 kDa), bovine serum albumin (BSA, 66 kDa) and equine myoglobin (17 kDa) were obtained from Sigma-Aldrich (Schnelldorf, Germany).
Rozova O.N., Khmelenina V.N., Bocharova K.A., Mustakhimov I.I, & Trotsenko Y.A. (2015). Role of NAD+-Dependent Malate Dehydrogenase in the Metabolism of Methylomicrobium alcaliphilum 20Z and Methylosinus trichosporium OB3b. Microorganisms, 3(1), 47-59.
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