Regulation of adenylate levels in intact spinach chloroplasts |
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Authors: | Y Kobayashi Y Inoue F Furuya K Shibata U Heber |
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Institution: | (1) Botanisches Institut der Universität, Schloßgarten 3, D-4400 Münster, Federal Republic of Germany |
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Abstract: | Starch phosphorylase activity in extracts of spinach or pea leaves and of isolated chloroplasts was determined and separated by electrophoresis in polyacrylamide gels. In spinach leaf extracts, a specific activity of 16 nmol glucose 1-phosphate formed per min per mg protein was found, whereas a lower value (6 nmol per min per mg protein) was observed in preparations of isolated chloroplasts which were about 75% intact. In the spinach leaf extracts two forms of phosphorylase were found; chloroplast preparations almost exclusively contained one of these. In pea leaf extracts the specific activity was 10 nmol glucose 1-phosphate formed per min per mg protein. Three forms of phosphorylase contributed to this activity. Preparations of isolated chloroplasts with an intactness of about 85% exhibited a lower specific activity (5nmol per min per mg protein) and contained two of these three phosphorylase forms.Abbreviations G1P
Glucose 1-phosphate
- Pi
orthophosphate
- Tris
Tris (hydroxymethyl)aminomethane
- MES
2(N-morpholino)ethane sulphonic acid
- EDTA
ethylenediamine tetraacetic acid
- HEPES
N-2-hydroxyethylpiperazine-N -2-ethanesulphonic acid |
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Keywords: | Pisum Spinacia Starch (metabolism phosphorylases) |
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