Nature of Incorporated 14C-Labeled Material Retained by Sulfuric Acid Fixed Bacteria in Pure Cultures and in Natural Aquatic Populations

1975 ◽  
Vol 32 (10) ◽  
pp. 1876-1879 ◽  
Author(s):  
John A. Baross ◽  
F. J. Hanus ◽  
Robert P. Griffiths ◽  
Richard Y. Morita
Keyword(s):  
Molecular Weight ◽  
Sulfuric Acid ◽  
Glutamic Acid ◽  
Fresh Water ◽  
Water Samples ◽  
Trichloroacetic Acid ◽  
Low Molecular Weight ◽  
Bacterial Populations ◽  
Membrane Filters ◽  
Pure Cultures

The levels of 14C-substrates (glutamic acid, alanine, glucose, and uracil) retained by aquatic bacteria in pure cultures and natural marine and fresh water samples after fixation with 2 N sulfuric acid (H2SO4 to reduce pH to 2) were found to be identical to the amount of 14C-labeled material associated with cold 10% trichloroacetic acid (TCA) precipitates collected on filters. Both TCA and H2SO4 were also equally effective in driving CO2 from solution. In heterotrophic potential studies, therefore, the 14C activity associated with natural bacterial populations collected on membrane filters after H2SO4 fixation represents macromolecules only, and not free substrate pools or low molecular weight metabolites.

scholarly journals The Genotoxicity of Caecal Water in Gilts Exposed to Low Doses of Zearalenone

Toxins ◽  
2018 ◽  
Vol 10 (9) ◽  
pp. 350 ◽  
Author(s):  
Katarzyna Cieplińska ◽  
Magdalena Gajęcka ◽  
Adriana Nowak ◽  
Michał Dąbrowski ◽  
Łukasz Zielonka ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Water Samples ◽  
Control Group ◽  
Low Molecular Weight ◽  
Low Doses ◽  
Vitro Analysis ◽  
Compensatory Effect ◽  
Control Group Group ◽  
In Vitro Analysis

Zearalenone is a toxic low-molecular-weight molecule that is naturally produced by moulds on crops as a secondary metabolite. The aim of this study was to determine the genotoxicity of caecal water collected successively from the caecal contents of gilts exposed to low doses (LOAEL, NOAEL, and MABEL) of zearalenone. The experiment was performed on 60 clinically healthy gilts with average BW of 14.5 ± 2 kg, divided into three experimental groups and a control group. Group ZEN5 were orally administered ZEN at 5 μg/kg BW, group ZEN10—10 μg ZEN/kg BW and group ZEN15—15 µg ZEN/kg BW. Five gilts from every group were euthanized on analytical dates 1, 2, and 3. Caecal water samples for in vitro analysis were collected from the ileocaecal region. The genotoxicity of caecal water was noted, particularly after date 1 in groups ZEN10 and ZEN15 with a decreasing trend. Electrophoresis revealed the presence of numerous comets without tails in groups C and ZEN5 and fewer comets with clearly expressed tails in groups ZEN10 and ZEN15. The distribution of LLC-PK1 cells ranged from 15% to 20% in groups C and ZEN5, and from 30% to 60% in groups ZEN10 and ZEN15. The analysis of caecal water genotoxicity during exposure to very low doses of ZEN revealed the presence of a counter response and a compensatory effect in gilts.

A L-glutamic acid based low molecular weight organogel as a vehicle for controlled drug release

2011 ◽  
Vol 41 (8) ◽  
pp. 1352-1358
Author(s):  
PengFei DUAN ◽  
MingHua LIU ◽  
Li ZHANG ◽  
YuanGang LI
Keyword(s):  
Molecular Weight ◽  
Drug Release ◽  
Glutamic Acid ◽  
Controlled Drug Release ◽  
Low Molecular Weight

scholarly journals The Fractionation of the Nitrogen Compounds of Wheat Flour on Sephadex Collumns

1968 ◽  
Vol 21 (5) ◽  
pp. 1077 ◽  
Author(s):  
HPC Galluse ◽  
AC Jennings
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Wheat Flour ◽  
Trichloroacetic Acid ◽  
Acid Water ◽  
Nitrogen Compounds ◽  
Low Molecular Weight ◽  
Acetic Acid Water

Bagdasarian et al. (1964) have discussed the difficulties in separating compounds of low molecular weight from proteins, and the advantages of using a volatile solvent, such as phenol~acetic acid~water (1 : 1 : 1, w/v/v) (referred to as solvent A in the remainder of this paper), to achieve this separation. Trichloroacetic acid is also efficient in effecting this separation (Bagdasarian et al. 1964), but it dissolves glycoproteins (Bell 1963; Stenzel et al. 1964 ; Jennings and Watt 1967) and some of the wheat flour proteins (Bell 1963) and is difficult to remove from solutions.

scholarly journals Comparative study of technologies for extraction of biologically active substances from the raw material of animal origin

2021 ◽  
Vol 6 (3) ◽  
pp. 226-235
Author(s):  
E. R. Vasilevskaya ◽  
M. A. Aryuzina ◽  
E. S. Vetrova
Keyword(s):  
Molecular Weight ◽  
Trichloroacetic Acid ◽  
Biologically Active Substances ◽  
Biologically Active ◽  
Animal Origin ◽  
Low Molecular Weight ◽  
Acid Extraction ◽  
Trichloroacetic Acid Solution ◽  
Wide Range ◽  
Active Substances

Technologies of isolation and concentration of biologically active substances, developed in the middle of the 20th century, need adjustment and adaptation to modern conditions both to increase the activity of substances and for greater economic efficiency. The aim of the research is the comparison of dynamics of biologically active compounds extraction from porcines pancreas in two methods: the saline method based on 0.9% sodium chloride solution, and the acidic method based on 2.4% trichloroacetic acid solution. Also the purpose of research is to assess the possibilities for further optimization of technologies. The total protein concentration based on the biuret reaction in the samples taken during the extraction, as well as the calculation and analysis of the point degrees and rates of extraction are chosen as the controlled parameters. Local maxima of the protein yields into the extractant media at the 60th, 135th and 255th minute were recorded during saline extraction; and at the 75th and 135th minute during acid extraction. Also the proteomic profile of the extracts was studied. Wide range of compounds with molecular weight of less than 52 kDa was found in extracts based on physiological saline solution, and protein substances of whole presented range of molecular weights in trichloroacetic acid based extracts were considered. The predominance of low molecular weight protein fraction of interest was noted also in this method of extraction in comparison with the other methods of extraction. According to the UniProt database, we assume availability of probable compounds with a molecular weight of less than 30 kDa in the purified acidic extract. The presence of some proteins absent in the final saline extract was noted. The acidic erythrograms showed a weak degrading effect of both types of extracts on the membranes of rat erythrocytes, as well as the cytoprotective effect of acidic ultrafiltrates (less than 3 kDa). The obtained results prove a better efficiency of trichloroacetic acid extraction method used for obtaining a mixture of a wide range of compounds, including biologically active substances of low molecular weight.

Preparation and Swelling Characteristics of Hydrogel from Microbial Low Molecular Weight Poly(γ-Glutamic Acid)

2014 ◽  
Vol 1028 ◽  
pp. 3-6
Author(s):  
Yu Bo Zhang ◽  
Zheng Li ◽  
Jian Fei Zhang ◽  
Chang Sheng Qiao
Keyword(s):  
Molecular Weight ◽  
Acid Solution ◽  
Glutamic Acid ◽  
Water Content ◽  
Chemical Method ◽  
High Water ◽  
Low Molecular Weight ◽  
Preparation Conditions ◽  
Swelling Characteristics ◽  
Crosslinker Concentration

In this paper, a novel low molecular weight poly (γ-glutamic acid) hydrogels were prepared by chemical method, and their preparation conditions such as poly (γ-glutamic acid) and crosslinker concentration, pH and temperature were studied. When poly (γ-glutamic acid) solution was 18%, pH 4.0, poly (γ-glutamic acid) was crosslinked to yield high water hydrogel with specific water content of 1328 times their dry volume depending on the preparation conditions.

Effects of Ultrasonic and Physical-Rays Treatment on the Molecular Structures of Poly(γ-Glutamic Acid)

2012 ◽  
Vol 518-523 ◽  
pp. 5550-5554
Author(s):  
Ming Hui ◽  
Chun Yuan Gao ◽  
Qing Tian ◽  
Xiao Bo Du ◽  
Xiang Long Yin
Keyword(s):  
Molecular Weight ◽  
Glutamic Acid ◽  
Molecular Weight Distribution ◽  
Weight Distribution ◽  
Molecular Structures ◽  
Low Molecular Weight ◽  
Chain Molecules ◽  
Sds Page ◽  
Γ Rays ◽  
Long Chain

Molecule structures of poly(γ-glutamic acid) (γ-PGA) were modified by ultrasonic, UV and 60Co γ-rays irradiation treatments, which might be used to prepare the polymer with low molecular weight. When 10 g/l γ-PGA solution was sonicated 60 times (400W, working time 3 s and interval 4 s) or that of 20 g/l solution was irradiated from 2 kGy to 10 kGy, the long-chain molecules were broken into smaller fragments. But, as the same solution of 10 g/l was irradiated by UV rays for 10 min, the molecular aggregates were observed in the solution so that the molecular weight distribution of γ-PGA became narrower compared with the control through the analysis of SDS-PAGE. These results would have a reference of the modification of γ-PGA molecules and the production of low molecular weight γ-PGA.

scholarly journals A study of the copper-binding proteins in liver and kidney tissue of neonatal normal and mottled mutant mice

1979 ◽  
Vol 183 (3) ◽  
pp. 721-730 ◽  
Author(s):  
A E Port ◽  
D M Hunt
Keyword(s):  
Molecular Weight ◽  
Glutamic Acid ◽  
Binding Proteins ◽  
Kidney Tissue ◽  
Weight Fraction ◽  
Exchange Chromatography ◽  
Low Molecular Weight ◽  
Copper Binding ◽  
Liver And Kidney ◽  
Cysteine Content

The Cu2+-binding proteins from liver and kidney tissue of 7–8-day-old brindled (Mobr) mice and their normal littermates were compared. (1) Separation over Bio-Gel P-10 showed that the differences in the Cu2+ content of mutant tissues were largely associated with a low-molecular-weight protein fraction (mol.wt. 14 500). (2) Further purification of this low-molecular-weight fraction by anion-exchange chromatography revealed four subfractions. The Cu2+ content of each subfraction reflected the Cu2+ status of the tissue of origin; the Cu2+ contents of the mutant kidney subfractions were elevated and those of the mutant liver were depressed compared with normal. In contrast, the protein contents of the subfractions were less variable and did not reflect the differing Cu2+ contents. (3) Amino acid analysis of the four subfractions from CuCl2-treated mutant and normal animals revealed clos similarities. The proteins showed high glycine, glutamic acid, serine, alanine and lysine contents and a rather variable cysteine content. Differences were apparent in the normal liver subfractions, which showed a higher cysteine content and lower glutamic acid content than did either the mutant liver or normal and mutant kidney subfractions. These observations, together with the recorded presence of aromatic amino acids, indicated that these proteins are not thioneins.

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