The influence of the peptide bond on the conformation of amino acids: A theoretical and FT-IR matrix-isolation study of N-acetylproline

2011 ◽  
Vol 159 (2-3) ◽  
pp. 247-256 ◽  
Author(s):  
Bram Boeckx ◽  
Riet Ramaekers ◽  
Guido Maes
Keyword(s):  
Amino Acids ◽  
Matrix Isolation ◽  
Peptide Bond ◽  
Ft Ir

The Kinetics of Inhibition of the Action of Thrombin by the Fibrinopeptides Formed during the Clotting of Fibrinogen

1966 ◽  
Vol 16 (01/02) ◽  
pp. 277-295 ◽  
Author(s):  
A Silver ◽  
M Murray
Keyword(s):  
Amino Acids ◽  
Competitive Inhibition ◽  
Amorphous Material ◽  
Peptide Bond ◽  
Initial Reaction ◽  
Reaction Products ◽  
Coagulation Mechanism ◽  
Kinetics Of ◽  
Kinetics Of Inhibition ◽  
Burk Plot

SummaryVarious investigators have separated the coagulation products formed when fibrinogen is clotted with thrombin and identified fibrinopeptides A and B. Two other peaks are observed in the chromatogram of the products of coagulation, but these have mostly been dismissed by other workers. They have been identified by us as amino acids, smaller peptides and amorphous material (37). We have re-chromatographed these peaks and identified several amino acids. In a closed system of fibrinogen and thrombin, the only reaction products should be fibrin and peptide A and peptide B. This reasoning has come about because thrombin has been reported to be specific for the glycyl-arginyl peptide bond. It is suggested that thrombin also breaks other peptide linkages and the Peptide A and Peptide B are attacked by thrombin to yield proteolytic products. Thrombin is therefore probably not specific for the glycyl-arginyl bond but will react on other linkages as well.If the aforementioned is correct then the fibrinopeptides A and B would cause an inhibition with the coagulation mechanism itself. We have shown that an inhibition does occur. We suggest that there is an autoinhibition to the clotting mechanism that might be a control mechanism in the human body.The experiment was designed for coagulation to occur under controlled conditions of temperature and time. Purified reactants were used. We assembled an apparatus to record visually the speed of the initial reaction, the rate of the reaction, and the density of the final clot formed after a specific time.The figures we derived made available to us data whereby we could calculate and plot the information to show the mechanism and suggest that such an inhibition does exist and also further suggest that it might be competitive.In order to prove true competitive inhibition it is necessary to fulfill the criteria of the Lineweaver-Burk plot. This has been done. We have also satisfied other criteria of Dixon (29) and Bergman (31) that suggest true competitive inhibition.

scholarly journals Recuperative Amino Acids Separation through Cellulose Derivative Membranes with Microporous Polypropylene Fiber Matrix

Membranes ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 429
Author(s):  
Aurelia Cristina Nechifor ◽  
Andreia Pîrțac ◽  
Paul Constantin Albu ◽  
Alexandra Raluca Grosu ◽  
Florina Dumitru ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cellulose Acetate ◽  
Polypropylene Fiber ◽  
Point Of View ◽  
Hydroxyethyl Cellulose ◽  
Separation Performance ◽  
Thermal Gravimetric Analyzer ◽  
Microfiltration Membranes ◽  
Ft Ir ◽  
Structural Point

The separation, concentration and transport of the amino acids through membranes have been continuously developed due to the multitude of interest amino acids of interest and the sources from which they must be recovered. At the same time, the types of membranes used in the sepa-ration of the amino acids are the most diverse: liquids, ion exchangers, inorganic, polymeric or composites. This paper addresses the recuperative separation of three amino acids (alanine, phe-nylalanine, and methionine) using membranes from cellulosic derivatives in polypropylene ma-trix. The microfiltration membranes (polypropylene hollow fibers) were impregnated with solu-tions of some cellulosic derivatives: cellulose acetate, 2-hydroxyethyl-cellulose, methyl 2-hydroxyethyl-celluloseand sodium carboxymethyl-cellulose. The obtained membranes were characterized in terms of the separation performance of the amino acids considered (retention, flux, and selectivity) and from a morphological and structural point of view: scanning electron microscopy (SEM), high resolution SEM (HR-SEM), Fourier transform infrared spectroscopy (FT-IR), energy dispersive spectroscopy (EDS) and thermal gravimetric analyzer (TGA). The re-sults obtained show that phenylalanine has the highest fluxes through all four types of mem-branes, followed by methionine and alanine. Of the four kinds of membrane, the most suitable for recuperative separation of the considered amino acids are those based on cellulose acetate and methyl 2-hydroxyethyl-cellulose.

Determination of ppb-Level CO, CO2, CH4, and H2O in High-Purity Gases Using Matrix Isolation FT-IR with an Integrating Sphere

1994 ◽  
Vol 66 (23) ◽  
pp. 4354-4358 ◽  
Author(s):  
Yoshimasa. Ogawara ◽  
Albert. Bruneau ◽  
Takako. Kimura
Keyword(s):  
High Purity ◽  
Matrix Isolation ◽  
Integrating Sphere ◽  
Ft Ir

scholarly journals Alum Catalyzed Simple, Efficient, and Green Synthesis of 2-[3-Amino-5-methyl-5-(pyridin-3-yl)-1,5-dihydro-4H-1,2,4-triazol-4-yl]propanoic Acid Derivatives in Aqueous Media

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Harshita Sachdeva ◽  
Diksha Dwivedi ◽  
Rekha Saroj
Keyword(s):  
Amino Acids ◽  
Green Chemistry ◽  
Green Synthesis ◽  
Aqueous Media ◽  
Propanoic Acid ◽  
Ft Ir ◽  
C Nmr

Alum (KAl(SO4)2·12H2O) is an inexpensive, efficient, and nontoxic catalyst used for the synthesis of 2-[3-amino-5-methyl-5-(pyridin-3-yl)-1,5-dihydro-4H-1,2,4-triazol-4-yl]propanoic acid derivatives in aqueous media by the reaction of 3-acetyl pyridine(1), amino acids(2)/(6), and thiosemicarbazide(4)at 80°C. This methodology offers significant improvements for the synthesis of products with regards to the yield of products, simplicity in operation, and green aspects by avoiding toxic catalysts which uphold the motto of green chemistry. Synthesized compounds have been characterized by FT-IR,13C NMR, and1HNMR spectroscopy.

scholarly journals Isolation, purification and structure of exochelin MS, the extracellular siderophore from Mycobacterium smegmatis

1995 ◽  
Vol 305 (1) ◽  
pp. 187-196 ◽  
Author(s):  
G J Sharman ◽  
D H Williams ◽  
D F Ewing ◽  
C Ratledge
Keyword(s):  
Amino Acids ◽  
Mycobacterium Smegmatis ◽  
Methyl Esters ◽  
Three Dimensional ◽  
Iron Chelation ◽  
Peptide Bond ◽  
Exchange Chromatography ◽  
Peptide Bonds ◽  
Hydrolysis Of ◽  
Gallium Complex

The extracellular siderophore from Mycobacterium smegmatis, exochelin MS, was isolated from iron-deficiently grown cultures and purified to > 98% by a combination of ion-exchange chromatography and h.p.l.c. The material is unextractable into organic solvents, is basic (pI = 9.3-9.5), has a lambda max at 420 nm and a probable Ks for Fe3+ of between 10(25) and 10(30). Its structure has been determined by examination of desferri- and ferri-exochelin and its gallium complex. The methods used were electrospray-m.s. and one- and two-dimensional (NOESY, DQF-COSY and TOCSY) 1H n.m.r. The constituent amino acids were examined by chiral g.l.c analysis of N-trifluoroacetyl isopropyl and N-pentafluoropropionyl methyl esters after hydrolysis, and reductive HI hydrolysis, of the siderophore. The exochelin is a formylated pentapeptide: N-(delta-N-formyl,delta N-hydroxy-R-ornithyl) -beta-alaninyl-delta N-hydroxy-R-ornithinyl-R-allo-threoninyl-delta N-hydroxy-S-ornithine. The linkages involving the three ornithine residues are via their delta N(OH) and alpha-CO groups leaving three free alpha-NH2 groups. Although there are two peptide bonds, these involve the three R (D)-amino acids. Thus the molecule has no conventional peptide bond, and this suggests that it will be resistant to peptidase hydrolysis. The co-ordination centre with Fe3+ is hexadenate in an octahedral structure involving the three hydroxamic acid groups. Molecular modelling shows it to have similar features to other ferric trihydroxamate siderophores whose three-dimensional structures have been established. The molecule is shown to have little flexibility around the iron chelation centre, although the terminal (Orn-3) residue, which is not involved in iron binding except at its delta N atom, has more motional freedom.

scholarly journals The rate-limiting step of protein synthesis in vivo and in vitro and the distribution of growing peptides between the puromycinlabile and puromycin-non-labile sites on polyribosomes

1971 ◽  
Vol 122 (3) ◽  
pp. 267-276 ◽  
Author(s):  
D. C. N. Earl ◽  
Susan T. Hindley
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Donor Site ◽  
Peptide Bond ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Donor And Acceptor ◽  
Rate Limiting

1. At 3 min after an intravenous injection of radioactive amino acids into the rat, the bulk of radioactivity associated with liver polyribosomes can be interpreted as growing peptides. 2. In an attempt to identify the rate-limiting step of protein synthesis in vivo and in vitro, use was made of the action of puromycin at 0°C, in releasing growing peptides only from the donor site, to study the distribution of growing peptides between the donor and acceptor sites. 3. Evidence is presented that all growing peptides in a population of liver polyribosomes labelled in vivo are similarly distributed between the donor and acceptor sites, and that the proportion released by puromycin is not an artifact of methodology. 4. The proportion released by puromycin is about 50% for both liver and muscle polyribosomes labelled in vivo, suggesting that neither the availability nor binding of aminoacyl-tRNA nor peptide bond synthesis nor translocation can limit the rate of protein synthesis in vivo. Attempts to alter this by starvation, hypophysectomy, growth hormone, alloxan, insulin and partial hepatectomy were unsuccessful. 5. Growing peptides on liver polyribosomes labelled in a cell-free system in vitro or by incubating hemidiaphragms in vitro were largely in the donor site, suggesting that either the availability or binding of aminoacyl-tRNA, or peptide bond synthesis, must be rate limiting in vitro and that the rate-limiting step differs from that in vivo. 6. Neither in vivo nor in the hemidiaphragm system in vitro was a correlation found between the proportion of growing peptides in the donor site and changes in the rate of incorporation of radioactivity into protein. This could indicate that the intracellular concentration of amino acids or aminoacyl-tRNA limits the rate of protein synthesis and that the increased incorporation results from a rise to a higher but still suboptimum concentration.

Gas Chromatographic/Matrix Isolation/Fourier Transform Infrared Spectra of the Laterally Chlorinated Dibenzo-p-Dioxins and Dibenzofurans

1989 ◽  
Vol 43 (8) ◽  
pp. 1317-1324 ◽  
Author(s):  
Charles J. Wurrey ◽  
Billy J. Fairless ◽  
Harry E. Kimball
Keyword(s):  
Fourier Transform ◽  
Infrared Spectra ◽  
Matrix Isolation ◽  
Fourier Transform Infrared ◽  
Fourier Transform Infrared Spectra ◽  
Reference Quality ◽  
Ft Ir ◽  
Chlorinated Dioxins ◽  
Chromatographic Matrix ◽  
Ft Ir Spectroscopy

Reference-quality gas chromatographic/matrix isolation/Fourier transform infrared spectra have been recorded for the following fifteen compounds, which collectively are referred to as the “laterally” chlorinated dibenzo- p-dioxins and dibenzofurans: 2,3,7,8-tetrachlorodibenzo- p-dioxin (2,3,7,8-TCDD); 1,2,3,7,8-pentachlorodibenzo- p-dioxin (1,2,3,7,8-PeCDD);l,2,3,4,7,8-hexachlorodibenzo- p-dioxin(1,2,3,4,7,8-HxCDD)>; 1,2,3,6,7,8,-hexachlorodibenzo- p-dioxin(1,2,3,6,7,8-HxCDD); 1,2,3,7,8,9-hexachlorodibenzo- p-dioxin (1,2,3,7,8,9-HxCDD); 1,2,3,4,6,7,8-heptachlorodibenzo- p-dioxin (1,2,3,4,6,7,8-HpCDD); 2,3,7,8-tetrachlorodibenzofuran (2,3,7,8-TCDF); 1,2,3,7,8-pentachlorodibenzofuran (1,2,3,7,8-PeCDF); 2,3,4,7,8-pentachlorodibenzofuran (2,3,4,7,8-PeCDF); 1,2,3,4,7,8-hexachlorodibenzofuran(1,2,3,4,7,8-HxCDF); 1,2,3,6,7,8-hexachlorodibenzofuran (1,2,3,6,7,8-HxCDF); 1,2,3,7,8,9-hexachlorodibenzofuran (1,2,3,7,8,9-HxCDF); 2,3,4,6,7,8-hexachlorodibenzofuran (2,3,4,6,7,8-HxCDF); 1,2,3,4,6,7,8-heptachlorodibenzofnran (1,2,3,4,6,7,8-HpCDF); and 1,2,3,4,7,8,9-heptachlorodibenzofuran (1,2,3,4,7,8,9-HpCDF). These spectra are discussed qualitatively and, for the laterally chlorinated dioxins, are compared to previously recorded gas-phase GC/FT-IR spectra. Estimates of the instrumental detection limits for these compounds, using matrix isolation GC/FT-IR spectroscopy, were found to fall in the mid-to-high picogram and low nanogram ranges.

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