The photoconversion of heat-treated Chenopodium chlorophyll protein and its pH dependence

スポンサーリンク

概要

• 論文の詳細を見る

• 1. Photosensitive Chenopodium chlorophyll protein was purified by warming the complex in a boiling water bath, followed by passing it through a Sephadex column. The shape and position of the absorption band in the absorption spectrum of purified chlorophyll protein (HCP668) were the same as those of non-treated chlorophyll protein (CP668), except for a change in the protein band in the UV region. The chlorophyll protein retained a quarter of its original photoconvertibility after heat treatment for 25 min at 100℃. Results suggested that the chlorophyll-amino acid residue binding is very stable against heat, and that chlorophyll is protected from decomposition through the rigid binding. 2. The photoconvertibility of HCP668, as well as CP668, depended strongly upon pH, with a pronounced decrease below pH 4 and above pH 6. Optimal convertibility was at pH 5. Above pH 12, convertibility vanished completely. However, pH-inhibited convertibility of HCP668 was recovered to its original level by returning the pH to neutral. 3 Illumination of CP668 in D_2O with red light caused a marked increase in light scattering. This reveals the occurrerence of a conformational change of apoprotein, leading to aggregation. 4. HCP668 was degraded by mechanical treatment to give a smaller size of photosensitive chlorophyll protein without loss of photoconvertibility. This small chlorophyll protein did not precipitate in a saturated (NH_4)_2SO_4 solution. The spectral properties of this complex were identical to those of HCP668 and CP668.

• 日本植物生理学会の論文

著者

• Yoshida Mizuki

  Institute Of Biophysics Faculty Of Agriculture Kyushu University

• Oku Tatsuo

  Institute Of Biophysics Faculty Of Agriculture Kyushu University

• Tomita Giiti

  Institute Of Biophysics Faculty Of Agriculture Kyushu University

• Oku Tatsuo

  Institute of Biophysics, Faculty of Agriculture, Kyushu University

関連論文

• Oxygen evolution in dark-developed spruce chloroplasts
• The reversible photoconversion of Chenopodium chlorophyll protein and its control by the apoprotein structure
• The Simultaneous Measurement of O2-Evolving and CO2-Fixing Activities in Fresh Leaves
• The photoconversion of heat-treated Chenopodium chlorophyll protein and its pH dependence
• Heat stability of the phototransforming activity of Chenopodium chlorophyll protein
• The Hill reaction and oxygen uptake in isolated pine chloroplasts
• Development of photosynthetic activities in dark-grown spruce seedlings
• Effects of nucleotides on the Hill reaction in aged chloroplasts
• Photosynthetic CO_2-fixing activity in dark-grown spruce seedlings
• Functional development of photosystems I and II in dark-grown pine seedlings
• Electron transfer and energy dependent reactions in glutaraldehyde-fixed chloroplasts
• Oligomycin-insensitive incorporation of ^P into chloroplast protein by illumination
• Changes of Time Courses of Delayed Fluorescence and Prompt Fluorescence during in vivo and in vitro Photoactivation of the Oxygen-evolving System in Dark-grown Spruce Seedlings

もっと見る 閉じる

スポンサーリンク