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Moll WA, de Wit B, Lutter R. Chlorophyllase activity in developing leaves of Phaseolus vulgaris L. Planta. 1978;139(1):79-83doi: 10.1007/BF00390814.
Moll, W. A., de Wit, B., & Lutter, R. (1978). Chlorophyllase activity in developing leaves of Phaseolus vulgaris L. Planta, 139(1), 79-83. https://doi.org/10.1007/BF00390814
Moll, W A, et al. "Chlorophyllase activity in developing leaves of Phaseolus vulgaris L." Planta vol. 139,1 (1978): 79-83. doi: https://doi.org/10.1007/BF00390814
Moll WA, de Wit B, Lutter R. Chlorophyllase activity in developing leaves of Phaseolus vulgaris L. Planta. 1978 Jan;139(1):79-83. doi: 10.1007/BF00390814. PMID: 24414110.
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Planta. 1978 Jan;139(1):79-83. doi: 10.1007/BF00390814.

Chlorophyllase activity in developing leaves of Phaseolus vulgaris L.

Planta

W A Moll, B de Wit, R Lutter

Affiliations

  1. Department of Plant Physiology, University of Amsterdam, IJdijk 26, Amsterdam, The Netherlands.

PMID: 24414110 DOI: 10.1007/BF00390814

Abstract

In crude extracts of primary leaves from dark grown seedlings of Phaseolus vulgaris L., relatively high hydrolytic activity of chlorophyllase (chlorophyll-chlorophyllido-hydrolase, EC 3.1.1.14) was observed. When plants were exposed to continuous illumination, the enzyme activity in the extracts was doubled within 3 days and both chlorophyll a and b were synthesized. However, when exposed to periodic illumination (1 min light-59 min dark) the enzyme activity was doubled within 1 to 2 days and chlorophyll a was synthesized but the formation of chlorophyll b was suppressed. When plants were transferred from periodic illumination to continuous illumination chlorophyll b was synthesized but the activity of chlorophyllase declined. Chloramphenicol blocked the increase in enzyme activity independent of the light regimes, but cycloheximide inhibited the activity more effectively during growth in the light. The presence of chlorophyllase activity in the leaves is discussed in relation to the chlorophyll-proteins and the membranes known to be present in chloroplasts. It is suggested that the enzyme is synthesized on plastid ribosomes.

References

  1. Plant Physiol. 1971 May;47(5):609-18 - PubMed
  2. Biochem Biophys Res Commun. 1974 Sep 9;60(1):468-73 - PubMed
  3. Biochem Soc Trans. 1977;5(1):98-102 - PubMed
  4. Plant Physiol. 1972 Apr;49(4):619-26 - PubMed
  5. Plant Physiol. 1949 Jan;24(1):1-15 - PubMed

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