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Biochemical changes during germination and seedling growth in Cuscuta campestris
Authors:Denys J Charles  Madhav Singh  G G Sanwal
Institution:Dept. of Biochemistry, Lucknow Univ., Lucknow-226007, Uttar Pradesh, India.
Abstract:Changes in the contents of starch, protein, DNA, RNA, total phosphorus, acid soluble phosphorus and inorganic phosphorus, and in the activities of some enzymes of carbohydrate, amino acid, nucleic acid and phosphate metabolism were studied during the germination of Cuscuta campestris seeds. The results are expressed on per seed basis.
Starch content in Cuscuta seeds showed a steady decline with most of it depleted by the end of the eighth day of germination. Protein content increased with germination up to 48 h and then decreased. RNA and DNA contents increased to a maximal level on the fourth day of germination and then decreased. Total phosphorus in the seeds remained almost unchanged during the period of study. Both trichloroacetic acid soluble and inorganic phosphorus increased until the third day and then decreased. Phytin was rapidly hydrolyzed with little being detectable by the seventh day of germination. Glucose-6-phosphate dehydrogenase increased with germination, while fructose bisphosphate aldolase which is indispensable for glycolysis, decreased with germination. Ribonuclease and deoxyribonuclease increased till the third and fourth day, respectively, and then decreased. Aspartate and alanine aminotransferases showed a maximum on the second day and then decreased. Activities of alkaline fructose-1,6-bisphosphatase and phytase were absent in the dry seeds and appeared only on the second day of germination. Both α- and β-amylase activities were present in the dry seed.
Keywords:Acid and alkaline phosphatase  alanine aminotransferase  α-and β-amylase  angiosperm parasite  aspartate aminotransferase  deoxyribonuclease  fructose bisphosphate aldolase  glucose-6-phosphate dehydrogenase  isocitrate dehydrogenase  neutral and alkaline fructose bisphosphatase  phytase  ribonuclease  seed reserves  starch phosphorylase
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