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A mRNA for Membrane Form of Guanylyl Cyclase Is Expressed Exclusively in the Testis of the Sea Urchin Hemicentrotus pulcherrimus

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Title: A mRNA for Membrane Form of Guanylyl Cyclase Is Expressed Exclusively in the Testis of the Sea Urchin Hemicentrotus pulcherrimus
Authors: Shimizu, Takeshi Browse this author
Takeda, Kenji Browse this author
Furuya, Hirotaka Browse this author
Hoshino, Katsuaki Browse this author
Nomura, Kohji Browse this author
Suzuki, Norio Browse this author
Issue Date: Apr-1996
Publisher: 日本動物学会
Journal Title: Zoological Science
Volume: 13
Issue: 2
Start Page: 285
End Page: 294
Abstract: A cDNA clone encoding the membrane form of guanylyl cyclase was isolated from a Hemicentrotus pulcherrimus testis cDNA library and its nucleotide sequence was determined. The cDNA was 4123 bp long and an open reading frame predicted a protein of 1125 amino acids including an apparent signal peptide of 21 residues; a single transmembrane domain of 25 amino acids which divides the mature protein into an amino-terminal, extracellular domain of 485 amino acids and a carboxyl-teninal, intracellular domain of 594 amino acids. Three potential N-linked glycosylation sites were present in the extracellular domain. Northern blot analysis of poly(A)+RNA from testes, ovaries, eggs and embryos at various developmental stages showed that the cDNA encoding guanylyl cyclase hybridized to a mRNA of 4.4 kb from the testes. We developed a large scale purification method of the phosphorylated (131 kDa) and dephosphorylated (128 kDa) forms of the membrane-bound guanylyl cyclase from H. pulcherrimus spermatozoa. The purified 131 kDa and 128 kDa forms of the guanylyl cyclase contained 26.0 ±1.3 and 4.3 ±0.7 moles of phosphate per mot protein (mean ±S.D.; n=6), respectively. The amino-terminal amino acids of both the 131 kDa and 128 kDa forms of the guanylyl cyclase could not be detected, suggesting that they were blocked.
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/2115/32991
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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