Long Distance Transport in Macrocystis integrifolia
- 1 June 1979
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 63 (6) , 995-1002
- https://doi.org/10.1104/pp.63.6.995
Abstract
Long distance transport of 14C-labeled photoassimilate was studied in M. integrifolia Bory. Movement of label followed the source-sink relationship; mature blades closer to the holdfast with young 2.degree. and 3.degree. fronds transported mostly to the base, those closer to the frond apex transported mostly to the apex, and those in intermediate positions transported both acropetally basipetally. The velocity of movement of 14C as computed from study of intact fronds and exudate was in the range of 35-72 cm/h and these estimates are on the low side. The composition of the translocate as determined for intact fronds was the same as that determined from exudate analysis; this composition was nearly identical with that of the photosynthate (40-50% mannitol and 40-50% amino acids). Apparently, the exudate represents the sieve tube sap and there is little if any selectivity exercised in the loading and translocation of photoassimilate. An analysis of translocated label in the growing apex is presented and indicates that the synthesis of polymeric compounds such as laminaran, alginate, cellulose, lipids and protein occurs in situ from the transported mannitol and amino acids. Detailed data on chemical composition of sieve tube sap from M. integrifolia and M. pyrifera (L.) C.A. Agardh are given and compared with the sieve tube sap from higher plants. Stipe segments, 60-100 cm long with 3-6 attached blades, are useful for translocation studies in Macrocystis.This publication has 4 references indexed in Scilit:
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- Eine Methode zur Dünnschichtchromatographischen Auftrennung von 14C- und 32P-markierten StoffwechselproduktenJournal of Chromatography A, 1969
- TRANSLOCATION IN THE GIANT KELP MACROCYSTIS I. RATES, DIRECTION, QUANTITY OF C14‐LABELED PRODUCTS AND FLUORESCEINJournal of Phycology, 1965
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951