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The Structure of the Junction between Short Subfragment-2 and the Hinge from Adult Chicken Smooth Muscle Myosin.


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Title: The Structure of the Junction between Short Subfragment-2 and the Hinge from Adult Chicken Smooth Muscle Myosin.
Other Titles: 成鶏平滑筋ショート・サブフラグメント‐2,ヒンジ連結領域の一次構造
Authors: Watanabe, Bunji / Tanigawa, Mihoko
Authors (alternative): 渡辺, 文治 / 谷川, 美保子
Issue Date: 31-Mar-1995
Citation: 長崎大学医療技術短期大学部紀要 = Bulletin of the School of Allied Medical Sciences, Nagasaki University. 1995, 8, p.1-8
Abstract: われわれは [Watanabe B (1989),Biol. Chem. Hoppe-Seyler 370 (9): 1027-1034 and Watanabe B, Tanigawa M (1993), Biol. Chem. Hoppe-Seyler 374 (1): 27-35]において成鶏の骨格筋,心室筋ミオシンのサブフラグメント‐2の構造と機能の関連性について発表したが,今回の論文は成鶏砂のう筋ミオシン(平滑筋)のショート・サブフラグメント‐2とヒンジとの連結部領域の構造を明らかにしたものである。 ミオシンをパパインで消化して得られた尾部(ロッド)をさらにα‐キモトリプシンで限定消化を行い,サブフラグメント‐2(S-2)とライトメロミオシン(LMM)に分離した。次いでサブフラグメント‐2のブロムシアン分解ペプチドの中から,ショート・サブフラグメント‐2のカルボキシ末端領域とヒンジのアミノ末端領域を含む134個のアミノ酸からなるペプチドを精製単離し,一次構造を決定した. さらに構造的相異を分析するために上記のようにして決定した連結部分の構造を胎鶏の砂のう筋(平滑筋),成鶏の脳,ドロソフィラ,成鶏骨格筋,成鶏心室筋ミオシンの相同部分の構造と比較した.その結果,興味あることに胎鶏の砂のう筋,成鶏の脳,ドロソフィラの非筋ミオシンとはそれぞれ100%,81.3%,59.7%の高いアミノ酸の同一性が認められ,これに対し成鶏骨格筋と成鶏心室筋ミオシンとはそれぞれ38.8%,40.3%と低いアミノ酸の同一性が認められた. / In the preceding papers [Watanabe B (1989), Biol. Chem. Hoppe-Seyler 370 (9): 1027-1034 and Watanabe B, Tanigawa M (1993), Biol. Chem. Hoppe-Seyler 374 (1): 27-35] we reported primary structures of subfragment-2 (S-2) from adult chicken skeletal and cardiac muscle myosins. This paper describes the structure of the junctional region between the short subfragment-2 (short S-2) and the hinge from adult chicken gizzard muscle myosin. The rod obtained by digesting myosin with papain was further subdivided into S-2 and light meromyosin (LMM) by limited digestion with α-chymotrypsin. A 134 amino-acid-residue peptide covered with carboxy-terminal portion of the short S-2 and amino-terminal portion of the hinge was isolated by conventional method from cyanogen bromide (CNBr) digests of S-2 and sequenced. To analyse the structural differences, the sequence of this junction thus determined was compared with those of corresponding portions of embryonic chicken gizzard, chicken brain, drosophila, chicken skeletal and chicken cardiac muscle myosin. Interestingly, results show the higher sequence identities of 100%, 81.3% and 59.7% with embryonic chicken gizzard, chicken brain and drosophila nonmuscle myosin, respectively, and lower degrees, 38.8% and 40.3% with chicken skeletal and chicken cardiac ventricular muscle myosin respectively.
Keywords: amino-acid sequence / primary structure / smooth muscle myosin / isoform / the short subfragment-2 / the hinge
URI: http://hdl.handle.net/10069/18228
ISSN: 09160841
Type: Departmental Bulletin Paper
Text Version: publisher
Appears in Collections:Volume 8

Citable URI : http://hdl.handle.net/10069/18228

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