Proteomics

Dataset Information

0

Scallop byssal protein identification


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 major SDS-PAGE fractions was treated with trypsin and analyzed using an Easy-nLC nanoflow HPLC system connected to an Orbitrap Elite 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 using Mascot v2.3.0 (Matrix Science, London, UK).

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Azumapecten Farreri

TISSUE(S): Byssus

SUBMITTER: Xiaokang Zhang  

LAB HEAD: Liu Weizhi

PROVIDER: PXD007932 | Pride | 2018-10-23

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
P16087-2-2.msf Msf
P16087-2-2.pep.pep.xml Pepxml
P16087-2-2.prot.prot.xml Xml
P16087-2-2.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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