Identification of three high molecular mass cysteine proteinases from rat skeletal muscle

FEBS Letters

Kuehn, L.¹  Dahlmann, B.¹  Reinauer, H.¹ 

[1] Diabetes Forschungsinstitut, Biochemical Department, Auf'm Hennekamp 65, 4000 Düsseldorf, FRG

关键词: Cysteine proteinase;    Alkaline;    High molecular mass;    Skeletal muscle (rat);   

DOI  :  10.1016/0014-5793(83)80975-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Three cysteine proteinases were isolated from the post-myofibrillar fraction of rat skeletal muscle. Proteinase I preferentially hydrolyzes Z-Phe—Arg-NMec with pH optimum at 8–9. The enzyme activity is stabilized by ATP against thermal inactivation. Proteinase II and III were not resolved by anion-exchange chromatography, by affinity chromatography on Arginine—Sepharose or by gel filtration. Proteinase II, splitting Bz-Val-Gly-Arg-NMec optimally at pH 10–10.5, is inactivated by ATP, whereas Proteinase III, hydrolyzing Suc-Ala-Ala-Phe-NMec at pH 7–7.5 is not affected by the nucleotide. The molecular mass of proteinase I is about 750 000 and that of proteinase II and III is about 650 000, as determined by gel filtration.

【 授权许可】

Unknown