Rapid primary structure determination of myoglobins by a complementary approach based on mass spectrometry and Edman degradation

Dosi, Roberta; Carusone, Annamaria; Severino, Valeria; Parente, Augusto; Maro, Antimo Di

doi:10.1016/j.foodchem.2012.02.042

Cited by 18 publications

(12 citation statements)

References 37 publications

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“…The primary structure of common pheasant Mb was determined by using a comparative peptide mapping strategy based on MALDI‐TOF mass spectrometry (Dosi et al, ).…”

Section: Resultsmentioning

confidence: 99%

“…Materials used for chromatographic separations were described elsewhere (Dosi et al, ). Standard proteins for SDS‐PAGE, trypsin (TPCK‐treated), and CNBr were purchased from Sigma‐Aldrich S.r.l.…”

Section: Methodsmentioning

confidence: 99%

“…Common pheasant Mb was purified from pheasant muscles as previously described (Di Giuseppe et al, ; Dosi et al, ). Briefly, meat samples (about 50 g) were homogenized at 4°C in MilliQ water (1:2; wt/vol) by using a Waring blender.…”

Section: Methodsmentioning

confidence: 99%

“…The separation of common pheasant apo‐Mb from the heme group was performed by reversed‐phase HPLC (RP‐HPLC) on a C‐4 column (4.6 × 150 mm, Alltech, Sedriano, Milan, Italy) as previously reported (Dosi et al, ).…”

Section: Methodsmentioning

confidence: 99%

“…Since the meat color, largely depending on Mb, is one of the properties that mostly influences the market value and consumer's purchase decision, many researches have been recently focused on the structural and functional characterization of Mb heme‐proteins from these birds. In particular, Japanese quail and northern bobwhite (Goodson, Beckstead, Payne, Singh, & Mohan, ), turkey (Joseph et al, ), ostrich (Dosi et al, ), and emu (Suman et al, ) Mbs have been characterized in the last years.…”

Section: Introductionmentioning

confidence: 99%

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Myoglobin from common pheasant (Phasianus colchicus L.): Purification and primary structure characterization

et al. 2017

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Myoglobin (Mb) is a monomeric hemoprotein involved in dioxygen storage and transport in skeletal muscles and heart. Mb, containing the heme pigment, is present in large amount in meat, thus influencing meat color and consumer choice. Here, the primary structure of Mb isolated from muscle of Phasianus colchicus L. was determined by using a comparative peptide mapping approach based on MALDI-TOF mass spectrometry. This strategy allowed the determination of common pheasant Mb primary sequence, which resulted identical to the chicken Mb, as also confirmed by intact molecular mass determination by ESI/Q-TOF mass spectrometry. Indeed, the accurate molecular mass (17,290.50 Da) of common pheasant Mb was found to be in good agreement with that of chicken Mb (17,290.86 Da). Finally, the 3D model of common pheasant Mb was predicted by homology modeling. Overall, in this study we confirmed that chicken, turkey and common pheasant, belonging to the Galliformes order, share the same Mb sequence. Practical applicationsConsidering the economic importance of game meat consumption, our result may be interesting for meat industry, providing useful information for the determination of species-specific differences in color and color stability compared to other poultry species.

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“…The primary structure of common pheasant Mb was determined by using a comparative peptide mapping strategy based on MALDI‐TOF mass spectrometry (Dosi et al, ).…”

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Myoglobin from common pheasant (Phasianus colchicus L.): Purification and primary structure characterization

et al. 2017

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Purification and Characterization of Novel Cationic Peroxidases from Asparagus acutifolius L. with Biotechnological Applications

et al. 2014

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Four novel basic peroxidases, named AaP-1, AaP-2, AaP-3, and AaP-4, were purified from Asparagus acutifolius L. seeds by cation-exchange and gel filtration chromatographies. The four proteins showed a similar electrophoretic mobility of 46 kDa while, by MALDI-TOF MS, different Mr values of 42758.3, 41586.9, 42796.3, and 41595.5 were determined for AaP-1, AaP-2, AaP-3, and AaP-4, respectively. N-terminal sequences of AaPs 1-4 up to residue 20 showed a high percentage of identity with the peroxidase from Glycine max. In addition, AaP-1, AaP-2, AaP-3, and AaP-4 were found to be glycoproteins, containing 21.75, 22.27, 25.62, and 18.31 % of carbohydrates, respectively. Peptide mapping and MALDI-TOF MS analysis of AaPs 1-4 showed that the structural differences between AaP-1 and AaP-2 and AaP-3 and AaPs-4 were mainly due to their glycan content. We also demonstrate that AaPs were able to remove phenolic compounds from olive oil mill wastewaters with a higher catalytic efficiency with respect to horseradish peroxidase, thus representing candidate enzymes for potential biotechnological applications in the environmental field.

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A New Antifungal Antibiotic from Bacillus sp. KM5 Isolated from Rice Rhizospheric Soil

Majumdar

Chakraborty

2017

Proc. Natl. Acad. Sci., India, Sect. B Biol. Sci.

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Rapid primary structure determination of myoglobins by a complementary approach based on mass spectrometry and Edman degradation

Cited by 18 publications

References 37 publications

Myoglobin from common pheasant (Phasianus colchicus L.): Purification and primary structure characterization

Myoglobin from common pheasant (Phasianus colchicus L.): Purification and primary structure characterization

Purification and Characterization of Novel Cationic Peroxidases from Asparagus acutifolius L. with Biotechnological Applications

A New Antifungal Antibiotic from Bacillus sp. KM5 Isolated from Rice Rhizospheric Soil

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