scholarly journals Subcellular Organization of the Cotyledons in Germinating Seeds and Seedlings of Pisum Sativum L.

1966 ◽  
Vol 19 (1) ◽  
pp. 69 ◽  
Author(s):  
Joan M Bain ◽  
FV Mercer
Keyword(s):  
Pisum Sativum ◽  
Ultrastructural Changes ◽  
Physiological Changes ◽  
Pisum Sativum L ◽  
Subcellular Organization ◽  
Cotyledon Cells ◽  
Germinating Seeds

Ultrastructural changes observed in pea cotyledon cells during germination of the seed and establishment of the seedling have been related to parallel anatomical and physiological changes in the cotyledons, observations being made at daily intervals up to the lOth day, and less frequently up to the 22nd day from planting. The changes have been related to three distinct phases recognized in the development of the seedling.

scholarly journals Subcellular Organization of the Developing Cotyledons of Pisum Sativum L.

1966 ◽  
Vol 19 (1) ◽  
pp. 49 ◽  
Author(s):  
Joan M Bain ◽  
FV Mercer
Keyword(s):  
Pisum Sativum ◽  
Fat Metabolism ◽  
Cell Formation ◽  
Physiological Changes ◽  
Pisum Sativum L ◽  
Parenchyma Cells ◽  
Subcellular Organization ◽  
Cell Organization ◽  
Developmental Phases ◽  
Storage Reserves

Morphological, anatomical, submicroscopical, and physiological changes in whole seeds and embryos of Pisum sativum L. cv. Victory Freezer were followed during 54 days of development of the seed. Four developmental phases-cell formation, cell expansion, synthesis of storage reserves, and maturation and dormancy-were recognized in the development of the embryo. Each phase was characterized by a distinctive physiology and a distinctive subcellular organization of the parenchyma cells. The subcellular organization associated with carbohydrate, protein, and fat metabolism and the significance of membranes in cell organization is described.

Leucyl β -Naphthylamidase Activities in Developing Seeds and Seedlings of Pisum sativum L

1977 ◽  
Vol 4 (4) ◽  
pp. 571 ◽  
Author(s):  
MD Collier ◽  
DR Murray
Keyword(s):  
Pisum Sativum ◽  
Maximum Rate ◽  
Storage Proteins ◽  
Total Activity ◽  
Selective Inhibitor ◽  
Cellular Proteins ◽  
Developing Seeds ◽  
Pisum Sativum L ◽  
Soluble Enzymes ◽  
Germinating Seeds

The activities of two soluble enzymes which hydrolyse L-leucyl �-naphthylamide have been measured in extracts from tissues of seeds and seedlings of Pisum sativum L. by using the chelator 1,10-phenanthroline as a selective inhibitor. In all the tissues studied, the phenanthroline-insensitive enzyme contributed the major proportion of the total activity against this substrate. In developing seeds, most of the activity of both enzymes is found in the maturing cotyledons, which develop maximum phenanthroline-sensitive and -insensitive activities respectively of 0.51 and 1.26 �mol per min per cotyledon (cv. Melbourne Market, dwarf) or 0.84 and 1.32 �mol per min per cotyledon (cv. Telephone, tall). In the cotyledons of germinating seeds, both enzyme activities increase within 24 h to values which are substantially lower than the maximum values found during development. These activities are maintained between 1 and 6 days from imbibition then they decline rapidly during the period of maximum rate of removal of protein from the cotyledon. The highest activities of both enzymes occur in tissues which are very active metabolically. This supports the view that they function as aminopeptidases in the general turnover of cellular proteins, rather than playing some additional specific role in the mobilization of storage proteins during germination.

Physiological Changes in Pea (Pisum sativum L. cv.Green Arrow) under NaCl Salinity

2006 ◽  
Vol 9 (5) ◽  
pp. 974-978 ◽  
Author(s):  
Najafi, F. ◽  
R.A. Khavari-Nejad . ◽  
F. Rastgar-jazii . ◽  
M. Sticklen .
Keyword(s):  
Pisum Sativum ◽  
Physiological Changes ◽  
Nacl Salinity ◽  
Pisum Sativum L

scholarly journals Effect of osmotic stress on in vitro translational capacity of polysomes and on the composition of polysome-associated proteins in germinating seeds of pea (Pisum sativum L.)

2012 ◽  
Vol 81 (3) ◽  
pp. 185-191 ◽  
Author(s):  
Wioletta Brosowska-Arendt ◽  
Stanisław Weidner
Keyword(s):  
Pisum Sativum ◽  
Osmotic Stress ◽  
Stress Proteins ◽  
Short Term ◽  
Pisum Sativum L ◽  
Associated Proteins ◽  
Total Pool ◽  
The Stability ◽  
Germinating Seeds

Plant growth throughout the world is often limited by unfavourable environmental conditions. This paper reports results of a study on long- and short-term osmotic stress (−0.5 MPa) followed by a recovery on in vitro translational capacity of polysomes and on the composition of polysome-associated proteins in germinating pea (<em>Pisum sativum </em>L.) seeds. Here we show that, under osmotic stress, cytoskeleton-bound polysomes were charaterized by the highest translation activity, which may be indicative of an important role that this population of polysomes plays in the synthesis of the so-called “stress proteins”. We also find out that in response to osmotic stress, new proteins (22.01, 96.47 and 105.3 kDa), absent in the unstressed sample, associated with the total pool of polysomes, whereas the protein of 22.95 kDa, which was present in the embryonic tissue of seeds germinating under unstressed conditions, disappeared. These changes may have affected both the stability and the translational capacity of polysomes.

scholarly journals The relationship of the Axis and the Cotyledons in Germinating Seeds and Seedlings of Pisum Sativum L.

1966 ◽  
Vol 19 (1) ◽  
pp. 85 ◽  
Author(s):  
Joan M Bain ◽  
FV Mercer
Keyword(s):  
Pisum Sativum ◽  
Complex Relation ◽  
Pisum Sativum L ◽  
Pea Seeds ◽  
Relationship Of ◽  
Germinating Seeds ◽  
The Relationship ◽  
Made In

Observations recorded extend previous investigations on changes occurring in cotyledons during the development of the seedling of Pisum sativum L., and were made in order to further understanding of the complex relation between the axis and cotyledons in germinating pea seeds and seedlings.

scholarly journals The major albumin proteins from pea (Pisum sativum L). Purification and some properties

1984 ◽  
Vol 218 (3) ◽  
pp. 795-803 ◽  
Author(s):  
R R D Croy ◽  
M S Hoque ◽  
J A Gatehouse ◽  
D Boulter
Keyword(s):  
Amino Acids ◽  
Pisum Sativum ◽  
Peptide Mapping ◽  
Cytosol Fraction ◽  
Preliminary Screening ◽  
Pisum Sativum L ◽  
Terminal Amino ◽  
Cnbr Cleavage ◽  
Sulphur Amino Acids ◽  
Cotyledon Cells

A scheme is described for the fractionation of pea (Pisum sativum) albumin proteins. By using this scheme, two closely related major albumin proteins have been isolated and purified to homogeneity. The larger protein, designated PMA-L, has Mr approximately 53 000 and consists of two 25 000-Mr subunits, whereas the smaller, PMA-S, has Mr approximately 48 000 and contains two 24 000-Mr subunits. There was no evidence of mixed dimers of the two subunit sizes, despite their close homology as judged by immunological crossreaction, amino acid composition, N-terminal amino acids, tryptic-peptide mapping and CNBr-cleavage products. Both proteins contained significant amounts of sulphur amino acids. The proteins were shown to be located in the soluble cytosol fraction of cotyledon cells and are not significantly degraded on seed germination. Preliminary screening indicates the presence of homologous major albumin proteins in at least three different, though closely related, legume species.

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