Developing the wool proteome

Clerens, Stefan; Cornellison, Charisa D.; Deb‐Choudhury, Santanu; Thomas, Ancy; Plowman, Jeffrey E.; Dyer, Jolon M.

doi:10.1016/j.jprot.2010.05.005

Cited by 37 publications

(43 citation statements)

References 16 publications

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“…These four MS/MS data sets (peak lists) were imported to the ProteinScape v3.1.0 proteomic data repository/bioinformatic software (Bruker Daltonics). Protein identification procedure was based on Clerens et al [50] with some modifications. For each of these mgf files, two types of sequence database searches were carried out against each of the two sequence databases: (1) [52,53].…”

Section: Protein Identificationmentioning

confidence: 99%

“…Annotated protein sequences were curated using CD-HIT-2D [56,57] against the NCBI O. aries protein sequence database (August 27, 2013; 30,406 sequences) [45]. Sequences that remained after curation were merged with the NCBI O. aries protein sequences (NCBI Taxonomy: 9940; August 27, 2013) and the in-house sheep protein sequences [50] to create a combined database for the final Mascot search. These Oar v3 sequences along with their corresponding representative sequences and their proposed names are listed in Supplementary Data 1a of Ref.…”

Section: Protein Identificationmentioning

confidence: 99%

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In-depth characterisation of the lamb meat proteome from longissimus lumborum

Morton

Clerens

et al. 2015

EuPA Open Proteomics

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Lamb MuscleMeat Proteomics a b s t r a c t Lamb is one of the major red meats consumed globally, both as a key component in the diet of some countries, and as a niche meat product in others. Despite this relatively wide consumption, an in-depth description of the global protein composition of lamb has not been reported. In this study, we investigated the proteome of the 48 h post-mortem lamb longissimus lumborum through separation of the samples into sarcoplasmic, myofibrillar and insoluble fractions, followed by an in-depth shotgun proteomic evaluation and bioinformatic analysis. As a result, 388 ovine-specific proteins were identified and characterised.The 207 proteins found in the sarcoplasmic fraction were dominated by glycolytic enzymes and mitochondrial proteins. This fraction also contained several sarcomeric proteins, e.g., myosin light chains and titin. Some of them might be the degradation products from the post-mortem proteolysis. Actin, myosin and tropomyosin were abundant in the myofibrillar fraction while nebulin and titin were also present. Collagen type I, III and IV were found in the insoluble fraction but there were also sequences from myosin and titin. The present study also confirms the existence of at least 300 predicted protein sequences obtained from the latest issue of the sheep genome (version 3) with high confidence.

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Section: Protein Identificationmentioning

confidence: 99%

Section: Protein Identificationmentioning

confidence: 99%

In-depth characterisation of the lamb meat proteome from longissimus lumborum

Morton

Clerens

et al. 2015

EuPA Open Proteomics

Self Cite

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show abstract

“…The protein fraction consists of a mixture of over a hundred proteins, mostly keratins (e.g. Clerens et al, 2010, Lee et al, 2006. The distribution of these proteins, and their crosslinking, varies between the different structures of the fibre (filament, matrix, medulla, cuticle: Koehn et al, 2010, Plowman et al, 2007.…”

Section: Introductionmentioning

confidence: 99%

An assessment of procedures to remove exogenous Sr before 87Sr/86Sr analysis of wet archaeological wool textiles

Holstein

Font

Peacock

et al. 2015

Journal of Archaeological Science

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“…AgResearch's ovine sequence information, coupled with recent non-gel proteomic work [28] has extended this database to the point where it rivals that of the human keratin database for the number of protein families and individual sequences that it contains. Armed with this database it has been possible for researchers to obtain a more complete mapping of the wool proteome than has been possible in the past [23,24].…”

Section: Discussionmentioning

confidence: 99%

“…2D-nanoflow LC-MS/MS was then performed on an Ultimate nanoflow HPLC (LC Packings, Amsterdam, Holland) interfaced with a QStar Pulsar i QqTOF mass spectrometer (Applied Biosystems, Foster City, CA, USA). The peptides were separated by 2D-LC-MS/MS in the first dimension on a strong cation exchange column and in the second a C18 column [28]. Identification and quantitation were carried out on a Mascot server.…”

Section: Itraq Quantitation Of Proteinsmentioning

confidence: 99%