Premium
Hydrophobicity of protochlorophyllide oxidoreductase, characterized by means of Triton X‐114 partitioning of isolated etioplast membrane fractions
Author(s) -
Selstam Eva,
WidellWigge Anna
Publication year - 1989
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1989.tb05660.x
Subject(s) - protochlorophyllide , oxidoreductase , membrane , biochemistry , biology , ultrastructure , chemistry , enzyme , botany
The inner etioplast membrane possesses a pronounced lateral heterogeneity with respect to protein and lipid composition as well as ultrastructural appearance. Little is known about the reason for formation of the regular branched structure shown by the prolamellar body part of the membrane. A specific interaction between the membrane lipids and the dominating protein NADPH‐protochlorophyllide oxidoreductase (PCR, EC 1.6.99.1) might be of major importance. In this study isolated prolamellar bodies and prothylakoids from the leaves of dark‐grown wheat ( Triticum aestivum L. cv. Starke II, Weibull) were exposed to Triton X‐114 partitioning in media with 150 m M NaCl and without. By comparing the partitioning of PCR, the ATP synthase (EC 3.6.1.3) polypeptides, and ribulosebisphosphate carboxylaseoxygenase (EC 4.1.1.39) in the different systems, it was concluded that PCR is an integral membrane protein with substantial hydrophilic domains.