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Mass Spectrometric Analysis of Phosphoserine Residues Conserved in the Catalytic Domain of Membrane-Bound Guanylyl Cyclase from the Sea Urchin Spermatozoa

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Title: Mass Spectrometric Analysis of Phosphoserine Residues Conserved in the Catalytic Domain of Membrane-Bound Guanylyl Cyclase from the Sea Urchin Spermatozoa
Authors: Furuya, Hirotaka Browse this author
Yoshino, Ken-ichi Browse this author
Shimizu, Takeshi Browse this author
Mantoku, Tsuyoshi Browse this author
Takeda, Tae Browse this author
Nomura, Kohji Browse this author
Suzuki, Norio Browse this author
Issue Date: Aug-1998
Publisher: 日本動物学会
Journal Title: Zoological Science
Volume: 15
Issue: 4
Start Page: 507
End Page: 516
Publisher DOI: 10.2108/0289-0003(1998)15[507:msaopr]2.0.co;2
Abstract: We have developed a large-scale purification method of the phosphorylated form (131 kDa) of membrane-bound guanylyl cyclase (mGC) from Hemicentrotus pulcherrimus spermatozoa. The purified mGC contained 26.0 ±1.3 moles of phosphate/mol enzyme (mean ±S.D., n = 6). Phosphorylated peptides were isolated from the trypsin digest of the carboxymethylated Hi. pulcherrimus sperm mGC by affinity chromatography on a Chelating Sepharose Fast Flow column, and the peptides were then subjected to mass spectrometric analysis and determination of phosphoserines, after the conversion of phosphoserines to S-ethylcysteines by amino acid analysis. Based on the observed mass number and the content of phosphoserine, serine residues at positions 561, 565, 652, 722, 740, 755, 894, 897, 914, 918, 927, 930, 951, and 985, in addition to two residues among those at positions 666, 670, and 671, were shown to be phosphorylated. They are all located in the intracellular region (kinase-like and catalytic domains). Notably, serine residues at positions 894, 918, 927, and 930, that are conserved in the sequence of mammalian mGCs and medaka fish-eye-specific mGCs, are phosphorylated in the sea urchin sperm mGC.
Rights: (c) 日本動物学会 / 本文献の公開は著者の意思に基づくものである
Relation: http://www.bioone.org/perlserv/?request=get-archive&issn=0289-0003
Type: article
URI: http://hdl.handle.net/2115/33001
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 鈴木 範男

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