Fractionation of hordein by preparative, continuous carrier-free electrophoresis

1968 ◽  
Vol 46 (10) ◽  
pp. 1301-1307 ◽  
Author(s):  
Ch. Ivanov ◽  
B. Mesrob ◽  
Z. Prusik
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acid Content ◽  
Amino Acid Content ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Basic Fraction ◽  
Acidic Amino Acids ◽  
Carrier Free ◽  
Terminal Amino

Barley hordein was fractionated by preparative, continuous carrier-free electrophoresis. Six fractions were obtained, one of which was in negligible quantity. Three of the fractions gave single symmetrical peaks. The amino acid content and the N-terminal amino acid residues of these fractions were determined. The ratios of basic to acidic amino acids showed that the fractions contained different protein substances. The most basic fraction, representing 10% of the total hordein, appeared to be pure since it contained only alanine as a N-terminal amino acid.

Evaluation of seed amino acid content and its correlation network analysis in wild soybean (Glycine soja) germplasm in Japan

2021 ◽  
Vol 19 (1) ◽  
pp. 35-43
Author(s):  
Awatsaya Chotekajorn ◽  
Takuyu Hashiguchi ◽  
Masatsugu Hashiguchi ◽  
Hidenori Tanaka ◽  
Ryo Akashi
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino Acid ◽  
Acid Content ◽  
Free Amino ◽  
Glycine Soja ◽  
Wild Soybean ◽  
Amino Acid Content ◽  
Soybean Seeds ◽  
Free Amino Acid Content

AbstractWild soybean (Glycine soja) is a valuable genetic resource for soybean improvement. Seed composition profiles provide beneficial information for the effective conservation and utilization of wild soybeans. Therefore, this study aimed to assess the variation in free amino acid abundance in the seeds of wild soybean germplasm collected in Japan. The free amino acid content in the seeds from 316 accessions of wild soybean ranged from 0.965 to 5.987 mg/g seed dry weight (DW), representing a 6.2-fold difference. Three amino acids had the highest coefficient of variation (CV): asparagine (1.15), histidine (0.95) and glutamine (0.94). Arginine (0.775 mg/g DW) was the predominant amino acid in wild soybean seeds, whereas the least abundant seed amino acid was glutamine (0.008 mg/g DW). A correlation network revealed significant positive relationships among most amino acids. Wild soybean seeds from different regions of origin had significantly different levels of several amino acids. In addition, a significant correlation between latitude and longitude of the collection sites and the total free amino acid content of seeds was observed. Our study reports diverse phenotypic data on the free amino acid content in seeds of wild soybean resources collected from throughout Japan. This information will be useful in conservation programmes for Japanese wild soybean and for the selection of accessions with favourable characteristics in future legume crop improvement efforts.

scholarly journals Deletion of the Actin-Associated Tropomyosin Tpm3 Leads to Reduced Cell Complexity in Cultured Hippocampal Neurons—New Insights into the Role of the C-Terminal Region of Tpm3.1

Cells ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 715
Author(s):  
Tamara Tomanić ◽  
Claire Martin ◽  
Holly Stefen ◽  
Esmeralda Parić ◽  
Peter Gunning ◽  
...  
Keyword(s):  
Amino Acid ◽  
Hippocampal Neurons ◽  
Molecular Mechanisms ◽  
Growth Cones ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
C Terminus ◽  
Primary Mouse ◽  
Terminal Amino

Tropomyosins (Tpms) have been described as master regulators of actin, with Tpm3 products shown to be involved in early developmental processes, and the Tpm3 isoform Tpm3.1 controlling changes in the size of neuronal growth cones and neurite growth. Here, we used primary mouse hippocampal neurons of C57/Bl6 wild type and Bl6Tpm3flox transgenic mice to carry out morphometric analyses in response to the absence of Tpm3 products, as well as to investigate the effect of C-terminal truncation on the ability of Tpm3.1 to modulate neuronal morphogenesis. We found that the knock-out of Tpm3 leads to decreased neurite length and complexity, and that the deletion of two amino acid residues at the C-terminus of Tpm3.1 leads to more detrimental changes in neurite morphology than the deletion of six amino acid residues. We also found that Tpm3.1 that lacks the 6 C-terminal amino acid residues does not associate with stress fibres, does not segregate to the tips of neurites, and does not impact the amount of the filamentous actin pool at the axonal growth cones, as opposed to Tpm3.1, which lacks the two C-terminal amino acid residues. Our study provides further insight into the role of both Tpm3 products and the C-terminus of Tpm3.1, and it forms the basis for future studies that aim to identify the molecular mechanisms underlying Tpm3.1 targeting to different subcellular compartments.

Importance of Terminal Amino Acid Residues to the Transport of Oligopeptides across the Caco-2 Cell Monolayer

2017 ◽  
Vol 65 (35) ◽  
pp. 7705-7712 ◽  
Author(s):  
Long Ding ◽  
Liying Wang ◽  
Zhipeng Yu ◽  
Sitong Ma ◽  
Zhiyang Du ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Monolayer ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Terminal Amino

scholarly journals Tamm–Horsfall urinary glycoprotein. The chemical composition

1970 ◽  
Vol 120 (2) ◽  
pp. 417-424 ◽  
Author(s):  
A. P. Fletcher ◽  
A. Neuberger ◽  
Wendy A. Ratcliffe
Keyword(s):  
Amino Acid ◽  
Performic Acid ◽  
Acid Oxidation ◽  
Amino Acid Residues ◽  
Carbohydrate Composition ◽  
Thiol Groups ◽  
Terminal Amino Acid ◽  
Cystine Content ◽  
Terminal Amino ◽  
Urinary Glycoprotein

1. A revised amino acid and carbohydrate composition of human Tamm–Horsfall glycoprotein is presented. 2. No significant differences were obtained in the amino acid composition of Tamm–Horsfall glycoprotein isolated from patients with cystic fibrosis. 3. The glycoprotein was shown to possess a high half-cystine content of 1 per 11–12 amino acid residues, which has been confirmed by performic acid oxidation and S-alkylation with iodoacetate and iodoacetamide. No thiol groups were detected in the glycoprotein. 4. Treatment of the glycoprotein with 0.5m-sodium hydroxide at 4°C for 2 days did not release heterosaccharide material, which suggests that the predominant carbohydrate–protein linkages present are not of the O-glycosidic type. 5. No N-terminal amino acid was detected in the glycoprotein.

Studies of the aminopeptidase proteolysis of semax analogues with different N-terminal amino acid residues

2011 ◽  
Vol 37 (4) ◽  
pp. 421-427 ◽  
Author(s):  
K. V. Shevchenko ◽  
T. V. V’yunova ◽  
I. Yu. Nagaev ◽  
L. A. Andreeva ◽  
L. Yu. Alfeeva ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Terminal Amino

scholarly journals 24-Epibrassinolide Restores the Synthesis of Proteins and Amino Acids in Brassica juncea L. Leaves Under Imidacloprid Stress

2017 ◽  
Vol 25 (2) ◽  
pp. 85-90 ◽  
Author(s):  
Anket Sharma ◽  
Vinod Kumar ◽  
Ashwani Kumar Thukral ◽  
Renu Bhardwaj
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Brassica Juncea ◽  
Total Protein ◽  
Acid Content ◽  
Soil Amendment ◽  
Insect Pests ◽  
Amino Acid Content ◽  
Total Proteins ◽  
Amino Acid Contents

Abstract Pesticides are applied to protect crops from a variety of insect pests but their application cause toxicity to plants that results, among others, in reduction of protein as well as amino acid contents. The present study is aimed at observing the effect of seed pre-soaking with 24-epibrassinolide (EBL) on the protein and amino acid content in the leaves of Brassica juncea L. grown in soil that is amended with pesticide im-idacloprid (IMI). Soil amendment with IMI resulted in a decrease in the contents in leaves of total proteins and 21 amino acids studied. Seed soaking with 100 nM of EBL resulted in the recovery of total protein as well as amino acid contents in leaves, when compared with plants grown in only IMI amended soils.

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