scholarly journals Domain structure and sequence distribution in dentin phosphophoryn

1991 ◽  
Vol 276 (3) ◽  
pp. 699-707 ◽  
Author(s):  
B Sabsay ◽  
W G Stetler-Stevenson ◽  
J H Lechner ◽  
A Veis
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Domain Structure ◽  
Peptide Sequencing ◽  
Cdna Libraries ◽  
Amino Acid Residues ◽  
Small Peptides ◽  
Sequence Distribution ◽  
Limited Digestion ◽  
Unique Composition

Phosphophoryn (PP) is a protein unique to the mineralized matrix of dentin. It also has a unique composition, with aspartic acid and phosphoserine comprising greater than 85% of all amino acid residues. Because of this unique composition and high content of phosphoserine, it has been difficult to apply direct peptide sequencing procedures effectively. However, to understand its function, and to prepare suitable probes for screening cDNA libraries, some sequence distribution information is required. To this end, using bovine (b) and rat incisor (ri) PPs, partial mild acid hydrolysis has been used to cleave at the aspartic acid residues and generate free amino acids and small peptides. The nature of the released amino acids and peptides has been determined. Peptides have also been generated by limited digestion with trypsin. Some of the peptides have been purified by h.p.l.c. techniques and sequenced. About 90% of the bPP and riPP were resistant to trypsin, and the large resistant fragment was sharply depleted of the non-aspartic acid and non-phosphoserine [(P)Ser] residues. All peptides isolated were acidic, but the remaining residues (other than aspartic acid and serine) appeared to be collected in regions flanking the trypsin-resistant core. These data show directly the presence of regions [Asp]n, [(P)Ser]m and [Asp-(P)Ser-Asp]k as prominent sequence features. A domain structure model is proposed.

Sequence analysis of a cDNA clone encoding the C-terminal end of human complement factor H

1987 ◽  
Vol 7 (3) ◽  
pp. 201-207 ◽  
Author(s):  
A. J. Day ◽  
J. Ripoche ◽  
A. Lyons ◽  
B. McIntosh ◽  
T. J. R. Harris ◽  
...  
Keyword(s):  
Amino Acids ◽  
Tertiary Structure ◽  
Regulatory Protein ◽  
Peptide Sequencing ◽  
Factor H ◽  
Cdna Libraries ◽  
Complement Factor ◽  
Protein Factor ◽  
The Complement System ◽  
Full Length Clone

Peptide sequencing of the complement system regulatory protein, factor H, permitted the synthesis of a mixed sequence oligonucleotide probe. Human liver cDNA libraries were screened and factor H-specific clones selected. No full-length clone was obtained, but the largest available clone, R2a, was found to encode the C-terminal 657 amino acids of factor H. The derived amino acid sequence consists of 10 contiguous internally homologous segments, each about 60 amino acids long. Sequences homologous to these are found in several other complement and non-complement proteins. Such sequences are likely to represent a particular type of tertiary structure subunit.

Arabidopsis and Lobelia anceps access small peptides as a nitrogen source for growth

2011 ◽  
Vol 38 (10) ◽  
pp. 788 ◽  
Author(s):  
Fiona M. Soper ◽  
Chanyarat Paungfoo-Lonhienne ◽  
Richard Brackin ◽  
Doris Rentsch ◽  
Susanne Schmidt ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nitrogen Source ◽  
Biomass Accumulation ◽  
Organic N ◽  
Amino Acid Residues ◽  
Growth Responses ◽  
Small Peptides ◽  
Inorganic N ◽  
Metabolic Products ◽  
Species Specific

While importance of amino acids as a nitrogen source for plants is increasingly recognised, other organic N sources including small peptides have received less attention. We assessed the capacity of functionally different species, annual and nonmycorrhizal Arabidopsis thaliana (L.) Heynh. (Brassicaceae) and perennial Lobelia anceps L.f. (Campanulaceae), to acquire, metabolise and use small peptides as a N source independent of symbionts. Plants were grown axenically on media supplemented with small peptides (2–4 amino acids), amino acids or inorganic N. In A. thaliana, peptides of up to four amino acid residues sustained growth and supported up to 74% of the maximum biomass accumulation achieved with inorganic N. Peptides also supported growth of L. anceps, but to a lesser extent. Using metabolite analysis, a proportion of the peptides supplied in the medium were detected intact in root and shoot tissue together with their metabolic products. Nitrogen source preferences, growth responses and shoot–root biomass allocation were species-specific and suggest caution in the use of Arabidopsis as the sole plant model. In particular, glycine peptides of increasing length induced effects ranging from complete inhibition to marked stimulation of root growth. This study contributes to emerging evidence that plants can acquire and metabolise organic N beyond amino acids.

Rates of Absorption by rat Intestine of Pancreatic Hydrolysates of Proteins and Their Corresponding Amino Acid Mixtures

1971 ◽  
Vol 41 (5) ◽  
pp. 409-417 ◽  
Author(s):  
R. F. Crampton ◽  
S. D. Gangolli ◽  
Pamela Simson ◽  
D. M. Matthews
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
High Capacity ◽  
Protein Digestion ◽  
Amino Acid Residues ◽  
Small Peptides ◽  
Rat Intestine ◽  
Protein Absorption ◽  
Amino Acid Mixtures ◽  
Mucosal Uptake

1. Though the occurrence of intestinal mucosal uptake of intact peptides, with cellular hydrolysis to amino acids, has been established, the importance of this mode of absorption in protein absorption is not known. This paper describes a comparison of the rates of intestinal absorption of pancreatic hydrolysates of four proteins with those of the corresponding acid hydrolysates or amino acid mixtures. 2. The results show that the absorption of pancreatic hydrolysates, consisting largely of small peptides of two to six amino acid residues, is substantially more rapid than that of the corresponding mixtures of free amino acids. This shows that the small intestine has a high capacity for absorption from mixtures of small peptides such as might be produced during protein digestion, and supports the hypothesis that mucosal uptake of intact oligopeptides is an important mode of protein absorption.

Effect of Glycylglycine on Absorption from Human Jejunum of an Amino Acid Mixture Simulating Casein and a Partial Enzymic Hydrolysate of Casein Containing Small Peptides

1977 ◽  
Vol 53 (1) ◽  
pp. 27-33
Author(s):  
P. D. Fairclough ◽  
D. B. A. Silk ◽  
M. L. Clark ◽  
D. M. Matthews ◽  
T. C. Marrs ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Acid Uptake ◽  
Amino Acid Residues ◽  
Small Peptides

1. A jejunal perfusion technique has been used in normal volunteer subjects to study jejunal absorption of amino acid residues from a partial enzymic hydrolysate of casein in which about 50% of the amino acids existed as small peptides, and also from an equivalent mixture of free amino acids. 2. The effect of a high concentration of the dipeptide glycylglycine on the absorption of amino acid residues from these preparations was studied to quantify the importance of mucosal uptake of intact peptides during absorption of the partial hydrolysate of casein. 3. The results were unexpected. Glycylglycine significantly inhibited absorption of several amino acid residues (aspartic acid + asparagine, serine, glutamic acid + glutamine, proline, alanine, phenylalanine, threonine and isoleucine) from the free amino acid mixture, whereas it significantly inhibited the absorption of only two (serine, glutamic acid + glutamine) from the peptide-containing partial casein hydrolysate. 4. The effect of glycylglycine on absorption of amino acids from the mixture of free amino acids was apparently due to inhibition of amino acid uptake by free glycine liberated from the dipeptide during perfusion. The reason for the failure of glycylglycine to cause extensive inhibition of absorption from the partial hydrolysate is not clear. It may be due to glycylglycine being only a weak inhibitor of peptide uptake, but the possibility that some peptides are taken up by a system unavailable to glycylglycine has to be considered.

Enzymatic Synthesis of 15N-L-aspartic Acid Using Recombinant Aspartase from Escherichia Coli K12

2008 ◽  
Vol 59 (11) ◽  
Author(s):  
Iulia Lupan ◽  
Sergiu Chira ◽  
Maria Chiriac ◽  
Nicolae Palibroda ◽  
Octavian Popescu
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Enzymatic Synthesis ◽  
Large Scale ◽  
Recombinant Dna ◽  
Industrial Enzymes ◽  
Recombinant Dna Technology ◽  
Bacterial Fermentation ◽  
Natural Protein ◽  
Novel Method

Amino acids are obtained by bacterial fermentation, extraction from natural protein or enzymatic synthesis from specific substrates. With the introduction of recombinant DNA technology, it has become possible to apply more rational approaches to enzymatic synthesis of amino acids. Aspartase (L-aspartate ammonia-lyase) catalyzes the reversible deamination of L-aspartic acid to yield fumaric acid and ammonia. It is one of the most important industrial enzymes used to produce L-aspartic acid on a large scale. Here we described a novel method for [15N] L-aspartic synthesis from fumarate and ammonia (15NH4Cl) using a recombinant aspartase.

13C nuclear magnetic resonance study of cyclodipeptides containing 13C enriched hydrophobic amino acids

1980 ◽  
Vol 45 (2) ◽  
pp. 482-490 ◽  
Author(s):  
Jaroslav Vičar ◽  
François Piriou ◽  
Pierre Fromageot ◽  
Karel Bláha ◽  
Serge Fermandjian
Keyword(s):  
Amino Acids ◽  
Nuclear Magnetic Resonance ◽  
Nuclear Magnetic Resonance Study ◽  
Coupling Constants ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Magnetic Resonance Study ◽  
Side Chain Conformation ◽  
13C Nuclear Magnetic Resonance ◽  
Hydrophobic Amino Acids

The diastereoisomeric pairs of cyclodipeptides cis- and trans-cyclo(Ala-Ala), cyclo(Ala-Phe), cyclo(Val-Val) and cyclo(Leu-Leu) containing 85% 13C enriched amino-acid residues were synthesized and their 13C-13C coupling constants were measured. The combination of 13C-13C and 1H-1H coupling constants enabled to estimate unequivocally the side chain conformation of the valine and leucine residues.

Post-proline endopeptidase, further characterization of the enzyme from pig kidneys

1984 ◽  
Vol 49 (8) ◽  
pp. 1846-1853 ◽  
Author(s):  
Karel Hauzer ◽  
Tomislav Barth ◽  
Linda Servítová ◽  
Karel Jošt
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Relative Molecular Mass ◽  
Enzyme Molecule ◽  
Thiol Compounds ◽  
Modified Method ◽  
N Terminus

A post-proline endopeptidase (EC 3.4.21.26) was isolated from pig kidneys using a modified method described earlier. The enzyme was further purified by ion exchange chromatography on DEAE-Sephacel. The final product contained about 95% of post-proline endopeptidase. The enzyme molecule consisted of one peptide chain with a relative molecular mass of 65 600 to 70 000, containing a large proportion of acidic and alifatic amino acids (glutamic acid, aspartic acid and leucine) and the N-terminus was formed by aspartic acid or asparagine. In order to prevent losses of enzyme activity, thiol compounds has to be added.

scholarly journals Selective Recognition of Amino Acids and Peptides by Small Supramolecular Receptors

Molecules ◽  
2020 ◽  
Vol 26 (1) ◽  
pp. 106
Author(s):  
Joana N. Martins ◽  
João Carlos Lima ◽  
Nuno Basílio
Keyword(s):  
Amino Acids ◽  
Selective Recognition ◽  
Great Promise ◽  
Macrocyclic Compounds ◽  
Synthetic Receptors ◽  
Small Peptides ◽  
Molecular Imprinted Polymers ◽  
Polymeric Systems ◽  
Physiological Conditions ◽  
Level Information

To this day, the recognition and high affinity binding of biomolecules in water by synthetic receptors remains challenging, while the necessity for systems for their sensing, transport and modulation persists. This problematic is prevalent for the recognition of peptides, which not only have key roles in many biochemical pathways, as well as having pharmacological and biotechnological applications, but also frequently serve as models for the study of proteins. Taking inspiration in nature and on the interactions that occur between several receptors and peptide sequences, many researchers have developed and applied a variety of different synthetic receptors, as is the case of macrocyclic compounds, molecular imprinted polymers, organometallic cages, among others, to bind amino acids, small peptides and proteins. In this critical review, we present and discuss selected examples of synthetic receptors for amino acids and peptides, with a greater focus on supramolecular receptors, which show great promise for the selective recognition of these biomolecules in physiological conditions. We decided to focus preferentially on small synthetic receptors (leaving out of this review high molecular weight polymeric systems) for which more detailed and accurate molecular level information regarding the main structural and thermodynamic features of the receptor biomolecule assemblies is available.

The potential mechanism of atmospheric new particle formation involving amino acids with multiple functional groups

2021 ◽  
Author(s):  
Jiarong Liu ◽  
Ling Liu ◽  
Hui Rong ◽  
Xiuhui Zhang
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Functional Groups ◽  
Atmospheric Aerosols ◽  
Potential Role ◽  
Particle Formation ◽  
Potential Mechanism ◽  
New Particle Formation

Amino acids are recognized as significant components of atmospheric aerosols. However, its potential role in the atmospheric new particle formation (NPF) is poorly understood, especially aspartic acid (ASP), one of...

The Xylem Sap of Maize Roots: Its Collection, Composition and Formation

1988 ◽  
Vol 15 (4) ◽  
pp. 557 ◽  
Author(s):  
MJ Canny ◽  
ME Mccully
Keyword(s):  
Amino Acids ◽  
Organic Acids ◽  
Organic Acid ◽  
Aspartic Acid ◽  
Xylem Sap ◽  
Great Variability ◽  
Reduced Pressure ◽  
Transpiration Stream ◽  
Maize Roots ◽  
Total Amino Acids

Three methods of sampling xylem sap of maize roots were compared: sap bleeding from the stem cut just above the ground; sap bleeding from the cut tops of roots still undisturbed in the ground; and sap aspirated from excavated roots under reduced pressure. The bleeding saps were often unobtainable. When their composition was measured with time from cutting, the concentrations of the major solutes approximately doubled in 2 h. Aspirated sap was chosen as the most reliable sample of root xylem contents. Solute concentrations of the saps showed great variability between individual roots for all solutes, but on average the concentrations found (in �mol g-1 sap) were: total amino acids, 1.8; nitrate, 1.8; sugars (mainly sucrose), 5.4; total organic acids, 18.3. Individual amino acids also varied greatly between roots. Glutamine, aspartic acid and serine were generally most abundant. The principal organic acid found was malic, approximately 8 �mol g-1. From these analyses the ratios of carbon in the fractions (sugars : amino acids : organic acids) = (44 : 6 : 50). 14Carbon pulse fed to a leaf appeared in the root sap within 30 min, rose to a peak at 4-6 h, and declined slowly over a week. During all this time the neutral, cation and anion fractions were sensibly constant in the proportions 86 : 10 : 4. The 14C therefore did not move towards the equilibrium of 12C-compounds in the sap. It is argued that the results do not support a hypothesis of formation of amino carbon from recent assimilate and reduced nitrate in the roots and an export of this to the shoot in the transpiration stream.

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