Light-induced changes in the distribution of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.) : I. Localization by immunoblotting in isolated plastids and total leaf extracts.

摘要: Changes in the relative content of NADPH-protochlorophyllide oxidoreductase during light-induced greening barley plants were measured both total leaf extract as well intact and broken plastids. The enzyme protein was identified by its apparent molecular weight immunological crossreactivity with an antiserum directed against oxidoreductase. monospecificity tested two different criteria: i. purified affinity chromatography. ii. It demonstrated that crossreacts only those polypeptides which appear to be enzymatically active. In fraction plastids isolated from leaves briefly illuminated concentration reduced drastically. Our results indicate this decrease is consequence artificial proteolytic breakdown membrane-bound protein. did not change dramatically first 4 6 h illumination. However, when exposure continuous white light extended further began decline rapidly while extracts remained almost constant for next 10 light. These part may localized outside plastid compartment.