Isolation of intact detergent‐free phycobilisomes by trypsin

FEBS Letters

Hiller, Roger G.²  Post, Adele²  Stewart, Alison C.¹ 

[1] School of Biological Sciences, University of Sydney, NSW 2006, Australia;School of Biological Sciences, Macquarie University, NSW 2113, Australia

关键词: Phycobilisome;    Biliprotein;    Fluorescence;    Trypsin;    (Griffithsia monilis);    (Rhodophyta);   

DOI  :  10.1016/0014-5793(83)80273-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phycobilisomes have been detached from red algal thylakoids by means of trypsin and purified by sucrosegradient centrifugation in the absence of detergents. These phycobilisomes have identical absorbance and fluorescence properties to phycobilisomes prepared with detergent. Their peptide composition determined by SDS-PAGE suggests that a lamellar peptide is cleaved by trypsin to release the intact phycobilisome. Subsequently trypsin attacks the 94 kDa peptide implicated [Redlinger, T. and Gantt, E. (1982) Proc. Natl. Acad. Sci. USA 79, 5542-5546] in the phycobilisome attachment.

【 授权许可】

Unknown