Localization of Thylakoid Membrane Enzyme, Chlorophyllase and Their Expression and Control

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Chlorophyllase was purified from leaves of Chenopodium album by several chromatographies. By the anion-exchange chromatography, the enzyme activity was separated three fractions, Types 1,2 and 3 with a molecular mass of 41.8,41.3, and 40.2 kDa, respectively.Amino acid analysis of N-terminus for the type 2 and 3 showed the same sequence. No homology for the amino acid sequence was obtained by computer search. Examination for optimum pH and Km for the Types 1 and 3 showed no difference between them. These proteins considered to be glycoprotein due to the adsorption onto lectin column. However, further study is necessary to confirm this. In this experiment, we were able to purify several types of chlorophyllase probably enough to rise antibody. We are now going to study on the localization of this enzyme in thylakoids membrane using its antibody and a cloning of gene of the enzyme.