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Comprehensive mapping of the bull sperm surface proteome

ABSTRACT: Nitrogen cavitation of bovine sperm to isolate plasma membrane. FASP digestion using trypsin. Data acquired using 5 workflows: (1) Unfractionated on a 5600 TripleTOF; (2) SCX-ESI-LC-MS/MS on a QSTAR Elite; (3) 1D Gel-LC-ESI-LC-MS/MS on a QSTAR Elite; (4) SCX-LC-MALDI-MS/MS on a UltrafleXtreme; (5) 1D Gel-LC-MALDI-MS/MS on a UltrafleXtreme

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Bos Taurus (bovine)

TISSUE(S): Spermatozoon

SUBMITTER: Michelle Colgrave

LAB HEAD: Michael K. Holland

PROVIDER: PXD000007 | Pride | 2020-01-27

REPOSITORIES: Pride

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			Action	DRS
	5600TF-BB1-SCX-1.wiff	Wiff
	5600TF-BB1-SCX-1.wiff.mtd	Wiff
	5600TF-BB1-SCX-1.wiff.scan	Wiff
	5600TF-BB1-SCX-10.wiff	Wiff
	5600TF-BB1-SCX-10.wiff.mtd	Wiff

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Comprehensive mapping of the bull sperm surface proteome.

Byrne Keren K Leahy Tamara T McCulloch Russell R Colgrave Michelle L ML Holland Michael K MK

Proteomics 20121122 23-24

While the mechanisms that underpin maturation, capacitation, and sperm-egg interactions remain elusive it is known that these essential fertilisation events are driven by the protein complement of the sperm surface. Understanding these processes is critical to the regulation of animal reproduction, but few studies have attempted to define the full repertoire of sperm surface proteins in animals of agricultural importance. Recent developments in proteomics technologies, subcellular fractionation, ...[more]

PMID: 23081703

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