Journal of Okayama Medical Association
Published by Okayama Medical Association

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Full-text articles are available 3 years after publication.

ラット肝ミトコンドリア・マトリクスのCa(2+)結合蛋白質の部分精製とその物性について

徳田 雅明 岡山大学医学部第一生理学教室
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抄録
A 193-fold purification of Ca(2+)-binding protein from rat liver mitochondrial matrix was achieved. The Ca(2+)-binding protein consisted of 3 polypeptide subunits whose respective molecular weights by SDS polyacrylamide gel electrophoresis were 62K, 49K and 37K. The molecular weight of the protein was 150K to 220K. The Kd for Ca(2+) was 1.3×10-(5)M and lower for Mn(2+) and Mg(2+). The protein was inactivated by heat treatment at 100℃ for 1 min, though stable against treatment with 0.5% w/v trypsin at 37℃ for 30 min. Ruthenium red did not inhibit Ca(2+)-binding.
キーワード
肝ミトコンドリア
Ca(2+)結合蛋白質
ISSN
0030-1558
NCID
AN00032489