Amino Acid Sequence of C-Terminal 17 kDa CNBr-Fragment of Akazara Scallop Troponin-I

• OJIMA Takao

  Department of Chemistry, Faculty of Fisheries, Hokkaido University

• TANAKA Hiroyuki

  Department of Chemistry, Faculty of Fisheries, Hokkaido University

• NISHITA Kyoyoshi

  Department of Chemistry, Faculty of Fisheries, Hokkaido University

抄録

The M_r 52, 000 subunit of Akazara scallop striated muscle troponin, which was tentatively identified as troponin I, was cleaved into two major fragments with CNBr: C-terminal 17 kDa fragment (CN17K) and N-terminal 35 kDa fragment (CN35K) [J. Biochem. 108, 519-521 (1990)]. CN17K inhibits rabbit reconstituted actomyosin Mg-ATPase activity, weakly in the absence of troponin T but strongly in its presence, together with Akazara tropomyosin. CN35K, however, hardly shows such inhibition. Thus, the amino acid sequence of the CN17K was determined by the Edman method. CN17K comprises 135 amino acid residues and its calculated molecular mass is 15, 732 Da. A computer search of the SWISS-PROT data base revealed the TnIs of crayfish tail muscle, rabbit skeletal muscle, and bovine cardiac muscle to be homologous proteins with total sequence homologies of 39, 30, and 30%, respectively, to CN17K. Significantly high homology was observed among these TnIs in the regions around residues 75-95, 99-114, and 135-151 of the rabbit TnI. From these facts, we conclude that the 52K subunit is a TnI.

収録刊行物

• The journal of biochemistry

  The journal of biochemistry 117 (1), 158-162, 1995-01-01

  社団法人 日本生化学会

キーワード

• amino acid sequence
• C-terminal 17kDa fragment
• 52 kDa troponing I
• scallop
• striated adductor muscle

詳細情報

• CRID: 1571135649327551360
• NII論文ID: 10005176579
• NII書誌ID: AA00694073
• ISSN: 0021924X
• Web Site: http://chemport.cas.org/cgi-bin/sdcgi?APP=ftslink&action=reflink&origin=jstage2&version=1.0&coi=1:CAS:528:DyaK2MXktVCmurY%3D&md5=5a033261b3397ec1e104ac63a34a895d
• 本文言語コード: en
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