Studies on the mechanism of action of D-amino acid transaminase

1994 ◽  
pp. 67-73
Author(s):  
James M. Manning
Keyword(s):  
Amino Acid ◽  
Mechanism Of Action

Amino acid-induced impairment of glucose oxidation by isolated rat muscle: mechanism of action

2007 ◽  
Vol 115 (S 1) ◽  
Author(s):  
K Stadlbauer ◽  
B Brunmair ◽  
Z Szöcs ◽  
M Krebs ◽  
A Luger ◽  
...  
Keyword(s):  
Amino Acid ◽  
Mechanism Of Action ◽  
Glucose Oxidation ◽  
Rat Muscle ◽  
Isolated Rat

The minimal amino acid sequence of the insulin-potentiating fragments of human growth hormone: its mechanism of action

Diabetes ◽  
1980 ◽  
Vol 29 (10) ◽  
pp. 782-787 ◽  
Author(s):  
F. M. Ng ◽  
J. Bornstein ◽  
C. E. Pullin ◽  
J. O. Bromley ◽  
S. L. Macaulay
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Growth Hormone ◽  
Mechanism Of Action ◽  
Human Growth

scholarly journals Studies on the Mechanism of Action of d-Amino Acid Oxidase

1971 ◽  
Vol 246 (22) ◽  
pp. 6855-6866 ◽  
Author(s):  
Christopher T. Walsh ◽  
Agnes Schonbrunn ◽  
Robert H. Abeles
Keyword(s):  
Amino Acid ◽  
Mechanism Of Action ◽  
Acid Oxidase ◽  
Amino Acid Oxidase

scholarly journals Beneficial Impacts of Incorporating the Non-Natural Amino Acid Azulenyl-Alanine into the Trp-Rich Antimicrobial Peptide buCATHL4B

Biomolecules ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 421
Author(s):  
Areetha R. D’Souza ◽  
Matthew R. Necelis ◽  
Alona Kulesha ◽  
Gregory A. Caputo ◽  
Olga V. Makhlynets
Keyword(s):  
Amino Acid ◽  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Mechanism Of Action ◽  
Bactericidal Activity ◽  
Antimicrobial Agents ◽  
Human Cells ◽  
Side Chains ◽  
Natural Amino Acid ◽  
Proteolytic Stability

Antimicrobial peptides (AMPs) present a promising scaffold for the development of potent antimicrobial agents. Substitution of tryptophan by non-natural amino acid Azulenyl-Alanine (AzAla) would allow studying the mechanism of action of AMPs by using unique properties of this amino acid, such as ability to be excited separately from tryptophan in a multi-Trp AMPs and environmental insensitivity. In this work, we investigate the effect of Trp→AzAla substitution in antimicrobial peptide buCATHL4B (contains three Trp side chains). We found that antimicrobial and bactericidal activity of the original peptide was preserved, while cytocompatibility with human cells and proteolytic stability was improved. We envision that AzAla will find applications as a tool for studies of the mechanism of action of AMPs. In addition, incorporation of this non-natural amino acid into AMP sequences could enhance their application properties.

Ru(II)-Based Amino Acid Complexes Show Promise for Leukemia Treatment: Cytotoxicity and Some Light on their Mechanism of Action

2019 ◽  
Vol 197 (1) ◽  
pp. 123-131
Author(s):  
Aliny Pereira de Lima ◽  
Marcio Aurélio Pinheiro Almeida ◽  
Francyelli Mello-Andrade ◽  
Flávia de Castro Pereira ◽  
Wanessa Carvalho Pires ◽  
...  
Keyword(s):  
Amino Acid ◽  
Mechanism Of Action ◽  
Amino Acid Complexes ◽  
Leukemia Treatment

scholarly journals Mechanism of action of rhatannin on plasma amino acid levels in rats.

1985 ◽  
Vol 33 (2) ◽  
pp. 715-721 ◽  
Author(s):  
TETSURO NAGASAWA ◽  
HIKOKICHI OURA ◽  
GENICHIRO NONAKA ◽  
ITSUO NISHIOKA
Keyword(s):  
Amino Acid ◽  
Mechanism Of Action ◽  
Plasma Amino Acid ◽  
Amino Acid Levels

scholarly journals Antibacterial Action of Structurally Diverse Cationic Peptides on Gram-Positive Bacteria

2000 ◽  
Vol 44 (8) ◽  
pp. 2086-2092 ◽  
Author(s):  
Carol L. Friedrich ◽  
Dianne Moyles ◽  
Terry J. Beveridge ◽  
Robert E. W. Hancock
Keyword(s):  
Amino Acid ◽  
Mechanism Of Action ◽  
Cytoplasmic Membrane ◽  
Membrane Depolarization ◽  
Membrane Permeabilization ◽  
Cationic Peptides ◽  
Nuclear Condensation ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Helical Peptide

ABSTRACT Antimicrobial cationic peptides are ubiquitous in nature and are thought to be a component of the first line of defense against infectious agents. It is widely believed that the killing mechanism of these peptides on bacteria involves an interaction with the cytoplasmic membrane. Cationic peptides from different structural classes were used in experiments withStaphylococcus aureus and other medically important gram-positive bacteria to gain insight into the mechanism of action. The membrane potential-sensitive fluorophore dipropylthiacarbocyanine was used to assess the interactions of selected antimicrobial peptides with the cytoplasmic membrane of S. aureus. Study of the kinetics of killing and membrane depolarization showed that, at early time points, membrane depolarization was incomplete, even when 90% or more of the bacteria had been killed. CP26, a 26-amino-acid α-helical peptide with a high MIC against S. aureus, still had the ability to permeabilize the membrane. Cytoplasmic-membrane permeabilization was a widespread ability and an action that may be necessary for reaching an intracellular target but in itself did not appear to be the killing mechanism. Transmission electron microscopy of S. aureus andStaphylococcus epidermidis treated with CP29 (a 26-amino-acid α-helical peptide), CP11CN (a 13-amino-acid, proline- and tryptophan-rich peptide), and Bac2A-NH2 (a linearized version of the 12-amino-acid loop peptide bactenecin) showed variability in effects on bacterial structure. Mesosome-like structures were seen to develop in S. aureus, whereas cell wall effects and mesosomes were seen with S. epidermidis. Nuclear condensation and abherrent septation were occasionally seen in S. epidermidis. Our experiments indicated that these peptides vary in their mechanisms of action and that the mechanism of action likely does not solely involve cytoplasmic-membrane permeabilization.

scholarly journals Amino acid requirement for the growth-hormone stimulation of incorporation of precursors into protein and nucleic acids of liver slices

1970 ◽  
Vol 119 (4) ◽  
pp. 629-634 ◽  
Author(s):  
M. J. Clemens ◽  
A. Korner
Keyword(s):  
Amino Acids ◽  
Growth Hormone ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Mechanism Of Action ◽  
Plasma Concentrations ◽  
Liver Slices ◽  
Hypophysectomized Rats ◽  
Stimulation Of

1. Incorporation of [14C]leucine into protein in rat liver slices, incubated in vitro, increased as the concentration of unlabelled amino acids in the incubation medium was raised. A plateau of incorporation was reached when the amino acid concentration was 6 times that present in rat plasma. Labelling of RNA by [3H]orotic acid was not stimulated by increased amino acid concentration in the incubation medium. 2. When amino acids were absent from the medium, or present at the normal plasma concentrations, no effect of added growth hormone on labelling of protein or RNA by precursor was observed. 3. When amino acids were present in the medium at 6 times the normal plasma concentrations addition of growth hormone stimulated incorporation of the appropriate labelled precursor into protein of liver slices from normal rats by 31%, and into RNA by 22%. A significant effect was seen at a hormone concentration as low as 10ng/ml. 4. Under the same conditions addition of growth hormone also stimulated protein labelling in liver slices from hypophysectomized rats. Tissue from hypophysectomized rats previously treated with growth hormone did not respond to growth hormone in vitro. 5. No effect of the hormone on the rate or extent of uptake of radioactive precursors into acid-soluble pools was found. 6. Cycloheximide completely abolished the hormone-induced increment in labelling of both RNA and protein. 7. It was concluded that, in the presence of an abundant amino acid supply, growth hormone can stimulate the synthesis of protein in rat liver slices by a mechanism that is more sensitive to cycloheximide than is the basal protein synthesis. The stimulation of RNA labelling observed in the presence of growth hormone may be a secondary consequence of the hormonal effect on protein synthesis. 8. The mechanism of action of growth hormone on liver protein synthesis in vitro was concluded to be similar to its mechanism of action in vivo.

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