Prevalence of the pit and antipit in the genus Glycine

1987 ◽  
Vol 45 ◽  
pp. 986-987
Author(s):  
R. W. Yaklich ◽  
E. L. Vigil ◽  
W. P. Wergin
Keyword(s):  
Amino Acids ◽  
Endoplasmic Reticulum ◽  
Glycine Max ◽  
Seed Coat ◽  
Cell Types ◽  
Abaxial Surface ◽  
Legume Seed ◽  
Initial Report ◽  
Cone Cells ◽  
Glycine Max L

The legume seed coat is the site of sucrose unloading and the metabolism of imported ureides and synthesis of amino acids for the developing embryo. The cell types directly responsible for these functions in the seed coat are not known. We recently described a convex layer of tissue on the inside surface of the soybean (Glycine max L. Merr.) seed coat that was termed “antipit” because it was in direct opposition to the concave pit on the abaxial surface of the cotyledon. Cone cells of the antipit contained numerous hypertrophied Golgi apparatus and laminated rough endoplasmic reticulum common to actively secreting cells. The initial report by Dzikowski (1936) described the morphology of the pit and antipit in G. max and found these structures in only 68 of the 169 seed accessions examined.

Reassessment of the pits and antipits in soybean seeds

2004 ◽  
Vol 82 (5) ◽  
pp. 654-662 ◽  
Author(s):  
Fengshan Ma ◽  
Carol A Peterson ◽  
Mark Gijzen
Keyword(s):  
Glycine Max ◽  
Seed Coat ◽  
Spherical Shape ◽  
Basic Structure ◽  
Aleurone Layer ◽  
Endosperm Tissue ◽  
Functional Aspects ◽  
Cone Cells ◽  
Inner Surface ◽  
Glycine Max L

A soybean (Glycine max (L.) Merr.) cotyledon has a concave region on its abaxial center called a pit, and the seed coat has a corresponding convex region on its inner surface called an antipit. While it is clear that the pit is lined with large epidermal cells, the anatomical identity of the antipit has been a subject of confusion. The inner surface of the seed coat consists of a compressed endosperm tissue that is subtended by an aleurone layer. In the antipit region of the seed coat, additional endosperm cells are situated between the aleurone layer and the compressed endosperm tissue. These endosperm cells, called cone cells, are similar to ordinary aleurone cells in basic structure. In the present study, it is demonstrated that the surface ornamentations of the antipit are a print of the pit on the compressed endosperm tissue. The functional aspects of the antipit–pit complex are not known. It was previously postulated that the antipit–pit region has an enhanced capability of nutrient translocation to the growing embryo, but there is little evidence to support this hypothesis. Alternatively, the antipit–pit association may provide a structural feature that anchors the embryo within the seed coat while contributing to an overall spherical shape of the seed.Key words: antipit, endosperm, Glycine max, pit, seed coat, soybean.

Effect of Phosphorus and Sulphur on Nutrient and Amino Acids Content of Soybean (Glycine max L. Merill) under ‘Alfisols’

2017 ◽  
Vol 16 (4) ◽  
pp. 1-7
Author(s):  
Sandeep Kumar ◽  
Javeed Wani ◽  
Bilal Lone ◽  
Asma Fayaz ◽  
Purshotam Singh ◽  
...  
Keyword(s):  
Amino Acids ◽  
Glycine Max ◽  
Glycine Max L

Effect of phosphorus and sulphur on nutrient and amino acids content of soybean [Glycine max (L.) Merill] under ‘Eutrochrepts’

2017 ◽  
Author(s):  
Sandeep Kumar ◽  
Javeed Ahmad Wani ◽  
Narinder Panotra ◽  
Bilal Ahmad Lone ◽  
Sameera Qayoom ◽  
...  
Keyword(s):  
Amino Acids ◽  
Glycine Max ◽  
Block Design ◽  
Soybean Seed ◽  
Omega 3 ◽  
Combined Application ◽  
Glycine Max L ◽  
Four Levels ◽  
Seed Application ◽  
Phosphorus Application

A field experiment was conducted at KVK, Srinagar during two consecutive kharif seasons of 2010 and 2011 to study the “Effect of phosphorus and sulphur on nutrient and amino acids content of soybean [Glycine max (L.) Merill] under Eutrochrepts”. The experiment was laid down under 16 treatment combinations viz four levels of phosphorus (0, 30, 60, 90 kg P2O5 ha-1) and four levels of sulphur (0, 15, 30, 45 kg S ha-1) in randomized complete block design with three replication . At higher levels of phosphorus application, Zn content of seed decreased and it was maximum at 30 kg P2O5 ha-1. With application of 45 kg S ha-1, N, P, K, Ca, Mg and S content in seed was 6.54, 0.555, 1.881, 0.329, 0.434 and 0.501 per cent respectively while as Zn, Fe, Cu, Mn was 109.99, 99.96, 2.82 and 3.73 mg kg-1, respectively. A significant interaction between P and S on macro as well as micronutrient content except Zn in seed was observed. Combined application of phosphorus and sulphur further enhanced the nutrient content of soybean seed. Combined application of phosphorus and sulphur enhanced the crude protein and oil content in soya seed 1. Individual as well as interaction effect of P and S was significant in enhancing the sulphur containing amino acids viz., cystine cystein and methionine content of soybean seed. Combined application of 45 kg S and 90 kg P2O5 ha-1 recorded significantly higher carbohydrate content (23.49%) in soybean seed. Application of increasing levels of phosphorus and sulphur resulted in gradual increase in linoleic (Omega-6) and linolenic acid (Omega-3).

Soluble phenolics and antioxidant properties of soybean (Glycine max L.) cultivars with varying seed coat colours

2013 ◽  
Vol 5 (3) ◽  
pp. 1065-1076 ◽  
Author(s):  
Kye Man Cho ◽  
Tae Joung Ha ◽  
Yong Bok Lee ◽  
Woo Duck Seo ◽  
Jun Young Kim ◽  
...  
Keyword(s):  
Glycine Max ◽  
Seed Coat ◽  
Antioxidant Properties ◽  
Soluble Phenolics ◽  
Glycine Max L

Regulation of the accumulation of β-Subunit of β-Conglycinin in nitrogen starved soybean (Glycine max L.) seed by amino acids and organic acids

2001 ◽  
pp. 132-133 ◽  
Author(s):  
N. Ohtake ◽  
S. Okano ◽  
T. Kawachi ◽  
H. Fujikake ◽  
K. Sueyoshi ◽  
...  
Keyword(s):  
Amino Acids ◽  
Glycine Max ◽  
Organic Acids ◽  
Β Subunit ◽  
Glycine Max L

scholarly journals The Relationship of the Contents of Calcium, Potassium and Pectin with Cracking of Seed Coat of Soybean (Glycine max (L.) Merr.)

2011 ◽  
Vol 80 (4) ◽  
pp. 433-440
Author(s):  
Takayo Saikusa ◽  
Shin-ichiro Kawase ◽  
Toshiroh Horino ◽  
Kyouko Toda ◽  
Yoshiyuki Nakamura
Keyword(s):  
Glycine Max ◽  
Seed Coat ◽  
Glycine Max L ◽  
Relationship Of ◽  
The Relationship

NSP-encoded reticulons, neuroendocrine proteins of a novel gene family associated with membranes of the endoplasmic reticulum

1994 ◽  
Vol 107 (9) ◽  
pp. 2403-2416 ◽  
Author(s):  
H.J. van de Velde ◽  
A.J. Roebroek ◽  
N.H. Senden ◽  
F.C. Ramaekers ◽  
W.J. Van de Ven
Keyword(s):  
Amino Acids ◽  
Endoplasmic Reticulum ◽  
Gene Family ◽  
Biochemical Characterization ◽  
Smooth Endoplasmic Reticulum ◽  
Dendritic Tree ◽  
Cell Types ◽  
In Vitro Translation ◽  
Amino Terminal

The novel NSP gene was previously shown to encode, among a variety of neuroendocrine cell types, two 3′-overlapping transcripts, a 3.4 kb one for NSP-A (776 amino acids) and a 1.8 kb one for NSP-C (208 amino acids). The deduced proteins, which were predicted to possess distinct amino-terminal regions, appeared to exhibit some architectural resemblance to known neuroendocrine proteins. In this paper the biochemical characterization and subcellular localization of the two proteins is addressed. In vitro translation of NSP-A and -C RNA produced proteins of about 135 and 23 kDa, respectively. Proteins of similar molecular mass were also detected in immunoprecipitation and western blot analyses of neural and endocrine cells using specific anti-NSP-A or -C antisera; some heterogeneity of NSP-A was observed. NSP-A, but not NSP-C, appeared to be highly phosphorylated and preferentially on serine residues. In immunocytochemical studies, we demonstrated that NSP-A and -C are associated with the endoplasmic reticulum; NSP-A was found to co-localize with SERCA2b, a membrane-associated Ca(2+)-ATPase of the endoplasmic reticulum. In Purkinje cells, we found NSP-immunostaining in the perikaryon, the extensive dendritic tree and the axon, also suggesting association with the smooth endoplasmic reticulum. Biochemical studies of NSP-A provided evidence that NSP-A is strongly associated with microsomal membranes and analysis of deletion mutants of NSP-A revealed that the hydrophobic carboxy-terminal portion of the protein, which is also present in NSP-C, is critical for membrane binding. Through database searches, finally, we found two different NSP-related sequences, one in a sequenced region of human chromosome 19, and the second in a human, pancreatic islet-derived partial cDNA, suggesting that the NSP gene is the prototype of a larger gene family. The results of our studies seem to indicate that the NSP-encoded proteins are novel, membrane-anchored components of the endoplasmic reticulum for which we propose the name reticulons.

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