Proteomics

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Scallop byssal protein identification, part 2

ABSTRACT: To explore the protein components for scallop byssus, the soluble fractions of scallop byssus was extract. For mass spectrometric analysis, proteins were extracted from byssal adhesive plaques, and the whole protein smple was treated with trypsin and analyzed using Thermo Fisher Q Exactive Mass Spectrometer (Thermo Fisher Scientific, USA). The mass spectrometry raw data were searched against the full set of predicted proteins from the C. farreri genome and Transcriptome using Mascot v2.3.0 (Matrix Science, London, UK).

INSTRUMENT(S): Q Exactive

ORGANISM(S): Azumapecten Farreri

TISSUE(S): Byssus

SUBMITTER: Xiaokang Zhang  

LAB HEAD: Weizhi liu

PROVIDER: PXD007987 | Pride | 2018-10-23

REPOSITORIES: pride

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bpi_6270_SHANBEI_01.raw Raw
bpi_6270_SHANBEI_01_02.raw Raw
bpi_6270_SHANBEI_02.raw Raw
bpi_6270_SHANBEI_02_02.raw Raw
bpi_6270_SHANBEI_03.raw Raw
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Publications

Bivalve molluscs are descendants of an early-Cambrian lineage superbly adapted to benthic filter feeding. Adaptations in form and behavior are well recognized, but the underlying molecular mechanisms are largely unknown. Here, we investigate the genome, various transcriptomes, and proteomes of the scallop Chlamys farreri, a semi-sessile bivalve with well-developed adductor muscle, sophisticated eyes, and remarkable neurotoxin resistance. The scallop's large striated muscle is energy-dynamic but  ...[more]

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