ePAD, an oocyte and early embryo-abundant peptidylarginine deiminase-like protein that localizes to egg cytoplasmic sheets

Selected for its high relative abundance, a protein spot of MW ∼75 kDa, p I 5.5 was cored from a Coomassie-stained two-dimensional gel of proteins from 2850 zona-free metaphase II mouse eggs and analyzed by tandem mass spectrometry (TMS), and novel microsequences were identified that indicated a pre...

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Veröffentlicht in:	Developmental biology 2003-04, Vol.256 (1), p.74-89
Hauptverfasser:	Wright, Paul W, Bolling, Laura C, Calvert, Meredith E, Sarmento, Olga F, Berkeley, Elizabeth V, Shea, Margaret C, Hao, Zhonglin, Jayes, Friederike C, Bush, Leigh Ann, Shetty, Jagathpala, Shore, Amy N, Reddi, Prabhakara P, Tung, Kenneth S, Samy, Eileen, Allietta, Margaretta M, Sherman, Nicholas E, Herr, John C, Coonrod, Scott A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Antibody Specificity Base Sequence Cleavage Stage, Ovum - enzymology Cloning, Molecular DNA, Complementary - genetics Female Gene Expression Regulation, Developmental Hydrolases - genetics Hydrolases - immunology Hydrolases - metabolism In Situ Hybridization Male Mice Mice, Inbred ICR Microscopy, Immunoelectron Molecular Sequence Data Oocytes - enzymology Oocytes - ultrastructure Ovary - enzymology Pregnancy Protein-Arginine Deiminases Recombinant Proteins - genetics Recombinant Proteins - immunology Recombinant Proteins - metabolism Sequence Homology, Amino Acid Solubility
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