FEBS Letters | |
Photoaffinity labeling of the lysosomal neuraminidase from bovine testis | |
Rose, Ursula1  Brossmer, Reinhard1  van der Horst, Gijsbertus T.J.2  Verheijen, Frans W.2  | |
[1] Department of Biochemistry II, University of Heidelberg, Heidelberg, Germany;Department of Cell Biology and Genetics, Erasmus University, Rotterdam, The Netherlands | |
关键词: Neuraminidase; Sialidase; Lysosomal; Photoaifinity labeling; ASA-NeuAc2en; 5-N-acetyl-9-(4-azidosalicoylamido)-2-deoxy-2; 3-didehydroneuraminic acid; IASA-NeuAc2en; 5-N-acetyl-9-(4-iodoazidosalicoylamido)-2-deoxy-2; 3-didehydroneuraminie acid; NeuAc2en; 2-deoxy-2; 3-didehydro-5-N-acetylneuraminic acid; MU-NeuAc; 2-α'-(4-methylumbelliferyl)-5-N-acetylneuraminic acid; SDS; sodium dodecyl sulfate; | |
DOI : 10.1016/0014-5793(90)80805-S | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
ASA-NeuAc2en, a photoreactive arylazide derivative of sialic acid, is shown to be a powerful competitive inhibitor of lysosomal neuraminidase from bovine testis (K i ≈ 21 μM). Photoaffinity labeling and partial purification of preparations containing this lysosomal neuraminidase activity result in specifically and non-specifically labeled polypeptides. Only labeling in a 55 kDa polypeptide is found to be specific, since it could be prevented by the competitive neuraminidase inhibitor NeuAc2en. We conclude that the 55 kDa polypeptide in the bovine testis β-galactosidase/neuraminidase/protective protein complex contains the catalytic site of neuraminidase.
【 授权许可】
Unknown
【 预 览 】
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