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FK506-binding Proteins from the Sirolimus Producer Streptomyces Hygroscopicus

Chun Chen, Lin Feng, Huang Jie, Chonghong Chen, Cheng Yuanrong

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Abstract

Objective To investigate how to isolate FK506\|binding proteins(FKBPs) from the sirolimus producer S.hygroscopicus. Methods The mycelial protein was prepared and isolated from S.hygroscopicus, and its peptidyl\|prolyl\|cis\|trans\|isomerase(PPIase) activity was determined. Results The protein pattern of S.hygroscopicus was obtained, and both 25 and 15 5 kD proteins possesed PPIase activity. Conclusion FKBP12 and FKBP25 in sirolimus producer S.hygroscopicus were quite different on Keller's report.\;

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Objective To investigate how to isolate FK506\|binding proteins(FKBPs) from the sirolimus producer S.hygroscopicus. Methods The mycelial protein was prepared and isolated from S.hygroscopicus, and its peptidyl\|prolyl\|cis\|trans\|isomerase(PPIase) activity was determined. Results The protein pattern of S.hygroscopicus was obtained, and both 25 and 15 5 kD proteins possesed PPIase activity. Conclusion FKBP12 and FKBP25 in sirolimus producer S.hygroscopicus were quite different on Keller's report.\;

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Available abstract

Objective To investigate how to isolate FK506\|binding proteins(FKBPs) from the sirolimus producer S.hygroscopicus. Methods The mycelial protein was prepared and isolated from S.hygroscopicus, and its peptidyl\|prolyl\|cis\|trans\|isomerase(PPIase) activity was determined. Results The protein pattern of S.hygroscopicus was obtained, and both 25 and 15 5 kD proteins possesed PPIase activity. Conclusion FKBP12 and FKBP25 in sirolimus producer S.hygroscopicus were quite different on Keller's report.\;

Key concepts: Streptomyces hygroscopicus, FKBP, Sirolimus, Chemistry, Rhizome, Isomerase, Biochemistry, Biology

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