Nutritional assessment of raw and germinated pea (Pisum sativum L.) protein and carbohydrate by in vitro and in vivo techniques

In vitro regeneration of pea (Pisum sativum L.), a regeneration recalcitrant legume, was optimised using thidiazuron. Buds were initiated from the meristems of the cotyledonary nodes of embryo axes, isolated from mature seeds, and subcultured on Murashige and Skoog medium supplemented with 13.3 μM 6-benzylaminopurine, 16.1 μM α-naphthaleneacetic acid, and 0.2 μM 2,3,5-triiodobenzoic acid. Proliferation of buds was preceded by the formation of white nodular-like protrusions. These structures were cut transversally in fine slices and subcultured on the same medium or in presence of thidiazuron that produces a second wave of secondary budding. The best results (90–110 buds per expiant) were obtained with 10 μM thidiazuron. The capacity of regeneration was genotype independent and reproducible. Buds elongated on the initial medium, then formed roots in presence of 5.37 μM α-naphthaleneacetic acid. and developed into viable plants. Key words: Pisum sativum L., regeneration, meristems, embryo axes, thidiazuron.

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Grafting in vitro Regenerated Pea (Pisum sativum L.) Shoots as a Method for Obtaining Mature Plants

Plant Breeding ◽

10.1111/j.1439-0523.1989.tb01267.x ◽

1989 ◽

Vol 102 (4) ◽

pp. 341-343 ◽

Cited By ~ 1

Author(s):

L. Natali ◽

A. Cavallini

Keyword(s):

Pisum Sativum ◽

Pisum Sativum L

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Protein synthesis in chloroplasts. Characteristics and products of protein synthesis in vitro in etioplasts and developing chloroplasts from pea leaves

Biochemical Journal ◽

10.1042/bj1460675 ◽

1975 ◽

Vol 146 (3) ◽

pp. 675-685 ◽

Cited By ~ 51

Author(s):

S G Siddell ◽

R J Ellis

Keyword(s):

Energy Source ◽

Protein Synthesis ◽

Large Subunit ◽

Sodium Dodecyl ◽

Supernatant Fraction ◽

Pisum Sativum L ◽

Fraction I ◽

Plastid Ribosomes

The function of plastid ribosomes in pea (Pisum sativum L.) was investigated by characterizing the products of protein synthesis in vitro in plastids isolated at different stages during the transition from etioplast to chloroplast. Etioplasts and plastids isolated after 24, 48 and 96h of greening in continuous white light, use added ATP to incorporate labelled amino acids into protein. Plastids isolated from greening leaves can also use light as the source of energy for protein synthesis. The labelled polypeptides synthesized in isolated plastids were analysed by electrophoresis in sodium dodecyl sulphate-ureapolyacrylamide gels. Six polypeptides are synthesized in etioplasts with ATP as energy source. Only one of these polypeptides is present in a 150 000g supernatant fraction. This polypeptide has been identified as the large subunit of Fraction I protein (3-phospho-D-glycerate carboxylyase EC 4.1.1.39) by comparing the tryptic ‘map’ of its L-(35S)methionine-labelled peptides with the tryptic ‘map’ of large subunit peptides from Fraction I labelled with L-(35S)methionine in vivo. The same gel pattern of six polypeptides is seen when plastids isolated from greening leaves are incubated with either added ATP or light as the energy source. However, the rates of synthesis of particular polypeptides are different in plastids isolated at different stages of the etioplast to chloroplast transition. The results support the idea that plastid ribosomes synthesize only a small number of proteins, and that the number and molecular weight of these proteins does not alter during the formation of chloroplasts from etioplasts.

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