Subtilisin enzymes: A note on time‐resolved fluorescence and circular dichroism properties

FEBS Letters

Janot, J.-M.¹  Martin, S.R.¹  Bayley, P.M.¹ 

[1] Division of Physical Biochemistry, National Institute for Medical Research, Mill Hill, London NW7 1AA, England

关键词: Subtilisin;    Tryptophan;    Fluorescence lifetime;    Anisotropy;    Segmental motion;    CD;   

DOI  :  10.1016/0014-5793(89)80762-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

This note briefly corrects previous information about the time-resolved fluorescence properties of preparations of subtilisin Carlsberg and subtilisin BPN′. We confirm the observation of segmental motion of the single tryptophan in subtilisin Carlsberg by analysis of the time-resolved fluorescence anisotropy, and present circular dichroism and spectroscopic data on the two proteins. Near-UV properties clearly differentiate between the two proteins. Far-UV circular dichroism confirms that the two subtilisins have closely similar secondary structure in solution; the multi-component analysis is consistent with the established X-ray conformations, but the quantitative agreement is still somewhat imperfect.

【 授权许可】

Unknown