Enzymatic-fluorometric analyses for glutamine, glutamate and free amino groups in protein-free plasma and milk

2017 ◽  
Vol 84 (1) ◽  
pp. 32-35 ◽  
Author(s):  
Torben Larsen ◽  
Carlos Fernández
Keyword(s):  
Glutamic Acid ◽  
Blood Plasma ◽  
High Throughput ◽  
Analytical Methods ◽  
Free Amino ◽  
Amino Groups ◽  
Technical Research ◽  
Animal Trials ◽  
Working Day ◽  
Free Plasma

This Technical Research Communication describes new analytical methods for free, unbound glutamic acid and glutamine in protein-free blood plasma and milk and introduces the use of quantitation of free amino groups in the same matrices for descriptive and analytical purposes. The present enzymatic-fluorometric methods are easily performed within one working day, allowing for ‘high throughput’ assays of animal trials. These assays could support and enable further studies in lactation physiology with the objective of improved metabolic health.

Peptidoglycan structure in cell walls of parental and filamentous Streptococcus cremoris HP

1974 ◽  
Vol 20 (7) ◽  
pp. 905-913 ◽  
Author(s):  
K. G. Johnson ◽  
I. J. McDonald
Keyword(s):  
Cell Wall ◽  
Glutamic Acid ◽  
Cell Walls ◽  
Free Amino ◽  
Muramic Acid ◽  
Chemical Analyses ◽  
Amino Groups ◽  
Streptococcus Cremoris ◽  
Peptidoglycan Structure ◽  
Filamentous Cell

Cell walls were prepared from parental and filamentous cells of Streptococcus cremoris HP. In addition to aspartic acid, glutamic acid, alanine, and lysine in a 1:2:3:1 ratio, such preparations contained hot formamide-extractable material composed of glucosamine, glucosa-mine-6-phosphate, glucose, galactose, and rhamnose. Parental and filamentous cell walls contained, respectively, 210 and 225 disaccharide units per milligram. The ratio of muramic acid: peptide subunits was about 1.3 for both preparations.Enzymic and chemical analyses revealed that glycan strands are incompletely substituted, peptide cross-bridging is not mediated by D-alanyl-L-alanyl linkages, peptide subunits are linked together to form large moieties, and no significant differences in peptidoglycan structure exist between parental and filamentous cell walls.Analysis by dinitrophenylation techniques disclosed the presence of significant quantities of glucosamine and muramic acid residues with free amino groups in the peptidoglycans of both cell wall preparations. Conversion of such groups by dinitrophenylation or N-acetylation greatly enhanced the response of cell walls to lysozyme digestion.

scholarly journals Quantitative Plasma Amino Acid Values in Leukemic Blood

Blood ◽  
1957 ◽  
Vol 12 (7) ◽  
pp. 635-643 ◽  
Author(s):  
JOHN J. KELLEY ◽  
HARRY A. WAISMAN
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Acute Leukemia ◽  
Glutamic Acid ◽  
Blood Plasma ◽  
Free Amino Acids ◽  
Free Amino ◽  
Quantitative Methods ◽  
Chronic Lymphatic Leukemia ◽  
Lymphatic Leukemia

Abstract 1. Quantitative methods for analysis of free amino acids in plasma have been performed on blood from normal and leukemic individuals. 2. An increase in the glutamic acid phenylalanine and "leucine" levels was found in the blood plasma of patients with acute leukemia. 3. Both the chronic myelogenous and the chronic lymphatic leukemia patients had high levels of glutamic acid, phenylalanine, alanine and proline. 4. Lower than normal levels of asparagine and threonine were found in the plasma of patients with acute leukemia.

COMPARATIVE STUDIES OF THE POTENTIATION OF CORTICOTROPHIN ACTIVITY BY SEVERAL INACTIVE DERIVATIVES

1963 ◽  
Vol 42 (2) ◽  
pp. 209-213 ◽  
Author(s):  
Arthur I. Cohen ◽  
Edward H. Frieden
Keyword(s):  
Biological Activity ◽  
Comparative Studies ◽  
Free Amino ◽  
Hormonal Activity ◽  
Amino Groups

ABSTRACT A number of corticotrophin analogues have been prepared, some of which potentiate the biological activity of the untreated hormone in vitro. The free amino groups of corticotrophin appear to be essential not only for hormonal activity, but also for the interaction of the analogues with the tissue corticotrophin inactivating system which is assumed to account for the potentiating effect.

scholarly journals FREE AMINO GROUPS OF EQUINE γ-GLOBULINS AND A SPECIFIC ANTIBODY

1955 ◽  
Vol 216 (2) ◽  
pp. 621-624
Author(s):  
Mary L. McFadden ◽  
Emil L. Smith
Keyword(s):  
Specific Antibody ◽  
Free Amino ◽  
Amino Groups ◽  
Γ Globulins

scholarly journals FREE AMINO GROUPS AND N-TERMINAL SEQUENCE OF RABBIT ANTIBODIES

1955 ◽  
Vol 214 (1) ◽  
pp. 185-196 ◽  
Author(s):  
Mary L. McFadden ◽  
Emil L. Smith
Keyword(s):  
Free Amino ◽  
Terminal Sequence ◽  
Amino Groups

scholarly journals Fast and Efficient 5′P Degradome Library Preparation for Analysis of Co-Translational Decay in Arabidopsis

Plants ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 466
Author(s):  
Marie-Christine Carpentier ◽  
Cécile Bousquet-Antonelli ◽  
Rémy Merret
Keyword(s):  
Gene Expression ◽  
Quality Control ◽  
Transcriptional Regulation ◽  
High Throughput ◽  
Library Preparation ◽  
Working Day ◽  
Set Up ◽  
Post Transcriptional Regulation ◽  
Commercial Kit

The recent development of high-throughput technologies based on RNA sequencing has allowed a better description of the role of post-transcriptional regulation in gene expression. In particular, the development of degradome approaches based on the capture of 5′monophosphate decay intermediates allows the discovery of a new decay pathway called co-translational mRNA decay. Thanks to these approaches, ribosome dynamics could now be revealed by analysis of 5′P reads accumulation. However, library preparation could be difficult to set-up for non-specialists. Here, we present a fast and efficient 5′P degradome library preparation for Arabidopsis samples. Our protocol was designed without commercial kit and gel purification and can be easily done in one working day. We demonstrated the robustness and the reproducibility of our protocol. Finally, we present the bioinformatic reads-outs necessary to assess library quality control.

An overview of analytical methods for monitoring bacterial transglycosylation

2014 ◽  
Vol 6 (19) ◽  
pp. 7590-7596 ◽  
Author(s):  
Bart Blanchaert ◽  
Erwin Adams ◽  
Ann Van Schepdael
Keyword(s):  
High Throughput ◽  
Analytical Methods ◽  
High Throughput Screens

This review highlights the fluorescence and radioactively labeled assays and high-throughput screens for the search for antibiotics targeting bacterial transglycosylation.

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