Preparation of biologically active ristocetin derivatives: replacements of the 1'-amino group

1985 ◽  
Vol 28 (9) ◽  
pp. 1371-1375 ◽  
Author(s):  
Thomas R. Herrin ◽  
Alford M. Thomas ◽  
Thomas J. Perun ◽  
James C. Mao ◽  
Stephen W. Fesik
Keyword(s):  
Biologically Active ◽  
Amino Group

scholarly journals Application of Asian pumpkin (Cucurbita ficifolia) serine proteinase for production of biologically active peptides from casein.

2013 ◽  
Vol 60 (1) ◽  
Author(s):  
Anna Dąbrowska ◽  
Marek Szołtysik ◽  
Konrad Babij ◽  
Marta Pokora ◽  
Aleksandra Zambrowicz ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Free Amino ◽  
Serine Proteinase ◽  
Biologically Active ◽  
Amino Group ◽  
Active Peptides ◽  
Rp Hplc ◽  
Amino Group Content ◽  
Biologically Active Peptides ◽  
Peptide Profiles

The main objective of this study was to determine potential application of a serine proteinase derived from Asian pumpkin for obtaining biologically active peptides from casein. The course of casein hydrolysis by three doses of the enzyme (50, 150, 300 U/mg of protein) was monitored for 24 hours by the determinations of: hydrolysis degree DH (%), free amino group content (μmole Gly/g), RP HPLC peptide profiles and by polyacrylamide gel electrophoresis. In all hydrolyzates analyzed antioxidant activities were determined using three tests: the ability to reduce iron ions in FRAP test, the ability to scavenge free radicals in DPPH test, and Fe(2+) chelating activity. The antimicrobial activity of obtained peptide fractions was determined as the ability to inhibit the growth of Escherichia coli, Bacillus cereus and Pseudomonas fluorescens in a diffusion plate test. The deepest degradation, expressed as the DH [%] and the free amino group content (67% and 7528 µmole Gly/mg, respectively), was noted in samples hydrolyzed with 300 U/ml of enzyme for 24 hours, while in other samples the determined values were about three and two times lower. The results were in agreement with the peptide profiles obtained by RP HPLC. The highest antioxidative activities determined in all tests were seen for the casein hydrolysate obtained with 300 U/mg protein of serine proteinase after 24 h of reaction (2.15 µM Trolox/mg, 96.15 µg Fe(3+)/mg, 814.97 µg Fe(2+)/mg). Antimicrobial activity was presented in three preparations. In other samples no antimicrobial activity was detected.

scholarly journals Biologically active macromolecular forms of oxytocin. [8-Lysine]oxytocin as a suitable ligand

1977 ◽  
Vol 165 (1) ◽  
pp. 43-47 ◽  
Author(s):  
C R Snell ◽  
D G Smyth
Keyword(s):  
Affinity Chromatography ◽  
Binding Proteins ◽  
Solid Support ◽  
Water Soluble ◽  
Biologically Active ◽  
Carboxyl Groups ◽  
Amino Group ◽  
Rat Uterus ◽  
Isolated Rat

[8-Lysine]oxytocin was synthesized on a solid support and possessed an oxytocic activity of 100 +/- 6 units mumol on the isolated rat uterus. The epsilon-carbamoyl, epsilon-3-carboxypropionyl and epsilon-3-carboxybutryl derivatives were prepared and had uterotonic activities of 400, 55 and 50 units/mumol respectively. [8-Lysine]oxytocin was coupled unambiguously through the epsilon-amino group to the carboxyl groups of carboxymethylated dextrans or epsilon-3-carboxypropionly-gelatin. The macromolecular oxytocins were water-soluble and retained signigicant oxytocic activity. [8-Lysine]oxytocin should prove a useful ligand for affinity chromatography of oxytocin-binding proteins.

scholarly journals The Importance of 6-Aminohexanoic Acid as a Hydrophobic, Flexible Structural Element

2021 ◽  
Vol 22 (22) ◽  
pp. 12122
Author(s):  
Agnieszka Markowska ◽  
Adam Roman Markowski ◽  
Iwona Jarocka-Karpowicz
Keyword(s):  
Amino Acid ◽  
Chemical Synthesis ◽  
Biologically Active ◽  
Flexible Structure ◽  
Amino Group ◽  
Structural Element ◽  
Synthetic Fibers ◽  
Active Structures ◽  
Modified Peptides

6-aminohexanoic acid is an ω-amino acid with a hydrophobic, flexible structure. Although the ω-amino acid in question is mainly used clinically as an antifibrinolytic drug, other applications are also interesting and important. This synthetic lysine derivative, without an α-amino group, plays a significant role in chemical synthesis of modified peptides and in the polyamide synthetic fibers (nylon) industry. It is also often used as a linker in various biologically active structures. This review concentrates on the role of 6-aminohexanoic acid in the structure of various molecules.

ChemInform Abstract: PREPARATION OF BIOLOGICALLY ACTIVE RISTOCETIN DERIVATIVES: REPLACEMENTS OF THE 1′-AMINO GROUP

1985 ◽  
Vol 16 (52) ◽  
Author(s):  
T. R. HERRIN ◽  
A. M. THOMAS ◽  
T. J. PERUN ◽  
J. C. MAO ◽  
S. W. FESIK
Keyword(s):  
Biologically Active ◽  
Amino Group

scholarly journals Synthesis, Characterization and Antimicrobial Properties of Schiff Bases Derived from Condensation of 8-Formyl-7-hydroxy-4-methylcoumarin and Substituted Triazole Derivatives

2009 ◽  
Vol 6 (s1) ◽  
pp. S239-S246 ◽  
Author(s):  
Kumar Sanjeev S. Lamani ◽  
Oblennavar Kotresh ◽  
Mohammed Shafi A. Phaniband ◽  
Jagannath C. Kadakol
Keyword(s):  
Schiff Base ◽  
Schiff Bases ◽  
Elemental Analysis ◽  
Mass Spectra ◽  
Biological Activities ◽  
Antimicrobial Properties ◽  
Biologically Active ◽  
Amino Group ◽  
H Nmr ◽  
Derivatives Of

Two biologically active classes of compounds coumarins and triazoles were employed to form the Schiff bases. The synthesized Schiff baseviz., 3-aryl-[(1-isocyano-4-methyl-7-hydroxycoumarin)]-5-methyl-1,3,4-triazoline-2-one and its substituents were obtained by the condensation of amino group of mono and disubstituted derivatives of 3-methyl-5-oxo-1,2, 4-triazoles with 8-formyl-7-hydroxy-4-methylcoumarin in alcohol. The characterization were studied by elemental analysis, IR,1H NMR and mass spectra. The biological activities of the compounds were assayed against two bacterial via,B. subtilis, E.coliand two fungal strainsA. niger, C.albican. The results indicate that the present compounds may serve as better fungicides when compared to bactericides. The synthesized compounds have turned to be wonder compounds possessing antimicrobial properties.

Characterization of photosystem II with the atomic-force microscope

1992 ◽  
Vol 50 (2) ◽  
pp. 1146-1147
Author(s):  
Kathleen M. Marr ◽  
Mary K. Lyon
Keyword(s):  
Photosystem Ii ◽  
Atomic Force Microscope ◽  
Three Dimensional ◽  
Biologically Active ◽  
Atomic Force ◽  
Freeze Etching ◽  
Image Averaging ◽  
Oxygen Evolving ◽  
Averaging Techniques

Photosystem II (PSII) is different from all other reaction centers in that it splits water to evolve oxygen and hydrogen ions. This unique ability to evolve oxygen is partly due to three oxygen evolving polypeptides (OEPs) associated with the PSII complex. Freeze etching on grana derived insideout membranes revealed that the OEPs contribute to the observed tetrameric nature of the PSIl particle; when the OEPs are removed, a distinct dimer emerges. Thus, the surface of the PSII complex changes dramatically upon removal of these polypeptides. The atomic force microscope (AFM) is ideal for examining surface topography. The instrument provides a topographical view of individual PSII complexes, giving relatively high resolution three-dimensional information without image averaging techniques. In addition, the use of a fluid cell allows a biologically active sample to be maintained under fully hydrated and physiologically buffered conditions. The OEPs associated with PSII may be sequentially removed, thereby changing the surface of the complex by one polypeptide at a time.

Depletion and Reconstitution of Active E. Coli Ribosomes

1975 ◽  
Vol 33 ◽  
pp. 640-641
Author(s):  
M. Boublik ◽  
W. Hellmann ◽  
F. Jenkins
Keyword(s):  
Protein Biosynthesis ◽  
Large Subunit ◽  
High Resolution Electron Microscopy ◽  
Small Subunit ◽  
Structure And Function ◽  
Biologically Active ◽  
Biological Macromolecules ◽  
E Coli ◽  
Resolution Electron ◽  
And Function

Correlations between structure and function of biological macromolecules have been studied intensively for many years, mostly by indirect methods. High resolution electron microscopy is a unique tool which can provide such information directly by comparing the conformation of biopolymers in their biologically active and inactive state. We have correlated the structure and function of ribosomes, ribonucleoprotein particles which are the site of protein biosynthesis. 70S E. coli ribosomes, used in this experiment, are composed of two subunits - large (50S) and small (30S). The large subunit consists of 34 proteins and two different ribonucleic acid molecules. The small subunit contains 21 proteins and one RNA molecule. All proteins (with the exception of L7 and L12) are present in one copy per ribosome.This study deals with the changes in the fine structure of E. coli ribosomes depleted of proteins L7 and L12. These proteins are unique in many aspects.

Fractionation of the Biologically Active Large Molecular Components of Human Gastric Content

1959 ◽  
Vol 37 (4) ◽  
pp. 439-444 ◽  
Author(s):  
Ranwel Caputto ◽  
William O. Smith ◽  
Jordan Tang ◽  
Raul E. Trucco ◽  
Walter Joel ◽  
...  
Keyword(s):  
Gastric Content ◽  
Biologically Active ◽  
Molecular Components

Bioavailability of naringenin chalcone in humans after ingestion of cherry tomatoes

2020 ◽  
Vol 90 (5-6) ◽  
pp. 411-416 ◽  
Author(s):  
Carina Kolot ◽  
Ana Rodriguez-Mateos ◽  
Rodrigo Feliciano ◽  
Katharina Bottermann ◽  
Wilhelm Stahl
Keyword(s):  
Plasma Levels ◽  
Average Concentration ◽  
Biologically Active ◽  
Thiol Groups ◽  
Structural Element ◽  
Active Molecule ◽  
Reactive Center ◽  
Average Maximum ◽  
Alpha Beta ◽  
Cherry Tomatoes

Abstract. Chalcones are a type of flavonoids characterized by an α-β unsaturated structural element which may react with thiol groups to activate pathways such as the Nrf2-Keap-1 system. Naringenin chalcone is abundant in the diet but little is known about its bioavailability. In this work, the bioavailability of naringenin chalcone from tomatoes was investigated in a group of healthy men (n=10). After ingestion of 600 grams of tomatoes providing a single dose of 17.3 mg naringenin chalcone, 0.2 mg of naringenin, and 195 mg naringin plasma levels of free and conjugated naringenin and naringenin chalcone (glucuronide and sulfate) were analyzed by UHPLC-QTOF-MS at 0.5, 1, 3, and 6 h post-consumption. Plasma levels of conjugated naringenin increased to about 12 nmol/L with a maximum at about 3 h. Concentrations of free naringenin hardly elevated above baseline. Plasma levels of free and conjugated naringenin chalcone significantly increased. A maximum of the conjugated chalcone was reached at about 3 h after ingestion with an average concentration of about 0.5 nmol/L. No free chalcone was detectable at baseline but low amounts of the unconjugated compound could be detected with an average maximum of 0.8 nmol/L at about 1 h after ingestion. The data demonstrate that naringenin chalcone is bioavailable in humans from cherry tomatoes as a dietary source. However, availability is poor and intramolecular cyclisation as well as extended metabolism likely contribute to the inactivation of the reactive alpha-beta unsaturated reactive center as well as the excretion of the biologically active molecule, respectively.

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