scholarly journals Some Researches on Histones

1962 ◽  
Vol 45 (4) ◽  
pp. 195-203 ◽  
Author(s):  
J. A. V. Butler
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Experimental Error ◽  
Tissue Specificity ◽  
Basic Amino Acid ◽  
Gel Chromatography ◽  
Rat Tissues ◽  
Calf Thymus ◽  
End Groups ◽  
Starch Gel

The histone extracted from calf thymus glands is a complex system of proteins, which can be fractionated by chromatography on carboxymethyl cellulose columns into three principal fractions (1) very lysine-rich, (2) moderately lysine-rich, (3) arginine-rich. When examined by starch gel chromatography each of these gives more than one band. Methods have been devised for further separation of the components in some cases. The components show characteristic differences in end groups and certain amino acids as well as in their basic character. Histones extracted from various rat tissues can be separated into similar fractions, of which the amino acid analyses are similar to those derived from calf thymus, within the experimental error. To this extent, no species or tissue specificity of the fractionated histones was observed. Although all the histone fractions contain approximately one basic amino acid to three non-basic amino acids their structure is not regular, as Phillips has shown that in certain fractions the number of non-basic groups between two basic groups may vary from 0 to seven or more. The possible functions of histones are discussed.

scholarly journals Synthesis of Organic Matter in Aqueous Environments Simulating Small Bodies in the Solar System and the Effects of Minerals on Amino Acid Formation

Life ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 32
Author(s):  
Walaa Elmasry ◽  
Yoko Kebukawa ◽  
Kensei Kobayashi
Keyword(s):  
Amino Acids ◽  
Organic Matter ◽  
Amino Acid ◽  
Solar System ◽  
Acid Formation ◽  
Gel Chromatography ◽  
Small Bodies ◽  
Enhanced Production ◽  
Aqueous Environments ◽  
Heating Duration

The extraterrestrial delivery of organics to primitive Earth has been supported by many laboratory and space experiments. Minerals played an important role in the evolution of meteoritic organic matter. In this study, we simulated aqueous alteration in small bodies by using a solution mixture of H2CO and NH3 in the presence of water at 150 °C under different heating durations, which produced amino acids after acid hydrolysis. Moreover, minerals were added to the previous mixture to examine their catalyzing/inhibiting impact on amino acid formation. Without minerals, glycine was the dominant amino acid obtained at 1 d of the heating experiment, while alanine and β-alanine increased significantly and became dominant after 3 to 7 d. Minerals enhanced the yield of amino acids at short heating duration (1 d); however, they induced their decomposition at longer heating duration (7 d). Additionally, montmorillonite enhanced amino acid production at 1 d, while olivine and serpentine enhanced production at 3 d. Molecular weight distribution in the whole of the products obtained by gel chromatography showed that minerals enhanced both decomposition and combination of molecules. Our results indicate that minerals affected the formation of amino acids in aqueous environments in small Solar System bodies and that the amino acids could have different response behaviors according to different minerals.

Basic amino acid induced isomerization of a spiropyran: towards visual recognition of basic amino acids in water

2007 ◽  
Vol 31 (11) ◽  
pp. 1878 ◽  
Author(s):  
Yuanyuan Liu ◽  
Meigong Fan ◽  
Shuxiao Zhang ◽  
Xiaohai Sheng ◽  
Jiannian Yao
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Visual Recognition ◽  
Basic Amino Acid ◽  
Basic Amino Acids

scholarly journals Amino Acid-Mediated Induction of the Basic Amino Acid-Specific Outer Membrane Porin OprD from Pseudomonas aeruginosa

1999 ◽  
Vol 181 (17) ◽  
pp. 5426-5432 ◽  
Author(s):  
Martina M. Ochs ◽  
Chung-Dar Lu ◽  
Robert E. W. Hancock ◽  
Ahmed T. Abdelal
Keyword(s):  
Amino Acids ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Regulatory Protein ◽  
Basic Amino Acid ◽  
Sole Source ◽  
Activation Mechanism ◽  
Beta Lactam ◽  
Mobility Shift ◽  
Carbon And Nitrogen

ABSTRACT Pseudomonas aeruginosa can utilize arginine and other amino acids as both carbon and nitrogen sources. Earlier studies have shown that the specific porin OprD facilitates the diffusion of basic amino acids as well as the structurally analogous beta-lactam antibiotic imipenem. The studies reported here showed that the expression of OprD was strongly induced when arginine, histidine, glutamate, or alanine served as the sole source of carbon. The addition of succinate exerted a negative effect on induction ofoprD, likely due to catabolite repression. The arginine-mediated induction was dependent on the regulatory protein ArgR, and binding of purified ArgR to its operator upstream of theoprD gene was demonstrated by gel mobility shift and DNase assays. The expression of OprD induced by glutamate as the carbon source, however, was independent of ArgR, indicating the presence of more than a single activation mechanism. In addition, it was observed that the levels of OprD responded strongly to glutamate and alanine as the sole sources of nitrogen. Thus, that the expression ofoprD is linked to both carbon and nitrogen metabolism ofPseudomonas aeruginosa.

scholarly journals Incorporation of 3H from δ-(l-α-amino (4,5-3H)adipyl)-l-cysteinyl-d-(4,4-3H)valine into isopenicillin N

1979 ◽  
Vol 184 (2) ◽  
pp. 421-426 ◽  
Author(s):  
J O'Sullivan ◽  
R C Bleaney ◽  
J A Huddleston ◽  
E P Abraham
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Adipic Acid ◽  
Experimental Error ◽  
Acid Oxidase ◽  
Cephalosporium Acremonium ◽  
Amino Acid Oxidase ◽  
Free System ◽  
A Cell ◽  
Isopenicillin N

1. delta-(L-alpha-Amino[4,5-3H]adipyl)-L-cysteinyl-D-[4,4-3H]valine has been synthesized from its constituent amino acids, the L-alpha-amino[4,5-3H]adipic acid being obtained by reduction with 3H2 of methyl 5-acetamido-5,5-diethoxycarbonylpent-2-enoate and subsequent decarboxylation and hydrolysis. 2. In a cell-free system prepared by lysis of protoplasts of Cephalosporium acremonium 3H was incorporated from the doubly labelled tripeptide into a compound that behaved like penicillin N or isopenicillin N. The relative specific radioactivities of the alpha-aminoadipyl and penicillamine moieties of the penicillin were the same (within experimental error) as those of the alpha-aminoadipic acid and valine residues respectively of the tripeptide. 3. The behaviour of the labelled alpha-aminoadipic acid from the penicillin to the L-amino acid oxidase of Crotalus adamanteus venom showed that it was mainly L-alpha-aminoadipic acid. 4. The results are consistent with the hypothesis that the carbon skeleton of the LLD-tripeptide is incorporated intact into the penicillin molecule and that the first product is isopenicillin N.

Influence of organic cations on basic amino-acid uptake by human placental villi

1995 ◽  
Vol 7 (6) ◽  
pp. 1491
Author(s):  
RB Krishna ◽  
J Dancis ◽  
M Levitz
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Basic Amino Acid ◽  
Amino Acid Uptake ◽  
Progressive Increase ◽  
Amino Acid Transporters ◽  
Acid Uptake ◽  
Chorionic Villi ◽  
Basic Amino Acids ◽  
Kinetics Of

Human placental chorionic villi were incubated for 30 min with [3H]lysine or [3H]arginine and the distribution ratios (intracellular:extracellular concentrations) were determined. The ratios remained unchanged when Na+ in Earle's buffered salt solution was replaced with Li+. When Na+ was replaced with choline there was a significant increase is distribution ratios (lysine 1.34 +/- 0.33 v. 3.99 +/- 0.15, arginine 1.95 +/- 0.37 v. 5.05 +/- 1.16). Leucine, a neutral amino acid with a Na(+)-independent transport system, was unaffected by choline substitution. The distribution ratio for alanine, which is Na(+)-dependent, was reduced (2.50 +/- 0.41 v. 1.45 +/- 0.20). Two other quarternary amines, acetyl-beta-methylcholine and tetraethylammonium chloride (TEA) caused similar increases in the distribution ratios of the basic amino acids. Hordenine, a tertiary amine, was less effective and there was little or no effect with ephedrine, a secondary amine. The choline effect was first observable at concentrations of 105 mM. With TEA, there was a progressive increase in distribution ratios beginning at 29 mM. Lysine efflux was measured after incubation of villi with lysine in Earle's buffer or choline buffer. Lysine was rapidly released to the fresh medium with 25% more retained in choline-exposed villi. The amines may cause alterations in the kinetics of basic amino-acid transporters or may modify other aspects of placental physiology permitting an increase retention of the basic amino acids.

scholarly journals Ehrlich chromogens, probable cross-links in elastin and collagen

1988 ◽  
Vol 252 (2) ◽  
pp. 387-393 ◽  
Author(s):  
P D Kemp ◽  
J E Scott
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Absorption Coefficient ◽  
Cross Linking ◽  
Diazonium Salts ◽  
Gel Chromatography ◽  
Skin Collagen ◽  
Cross Links ◽  
End Group ◽  
15N Abundance

(1) Proteolytic digests of tissue elastin contain material which reacts with dimethylaminobenzaldehyde in acid solution (Ehrlich's reagent) to give a cherry-pink colour. This Ehrlich chromogen(s) [EC(s)] is similar to but not identical with EC(s) previously demonstrated in tissue collagens [Scott, Hughes & Shuttleworth (1979) Biosci. Rep. 1, 611-618]. Both ECs react with diazonium salts in acid to give coloured products. (2) Diazobenzene linked via a phenolic ester to polyacrylamide beads (Biogel P10) has been used to absorb ECs specifically and almost quantitatively from proteolytic digests. The coupled deeply coloured azo-EC-peptides were then recovered after mild alkaline cleavage from the support and purified by gel chromatography. (3) Using 15N-labelled NaNO2, the collagen azo-EC-peptides were prepared, and 15N abundance measured therein. The molar absorption coefficient of the azo-EC group was calculated (18,700) based on the assumption that each azo-EC group contained one 15N atom. (4) Collagen azo-EC-peptides contained glucose and galactose, whereas elastin azo-EC peptides did not. The amino acid patterns of the two peptides were quite different, the former being rich in polar amino acids, the latter containing much alanine. The patterns were compatible with an origin from the cross-linking regions of collagen and elastin respectively. (5) Quantitative (molar) comparisons of the azo-EC group content with amino acid, amino end-group and sugar contents, and azo-EC peptide molecular mass, suggest that a structure is present in the collagen azo-EC-peptides containing two EC groups shared between four peptide chains. Three peptide chains probably meet at each (cross-linking) EC group. (6) Based on this structure, about 15% of adult bovine skin collagen contains EC groups.

Permeability and membrane transport in the larva of Taenia crassiceps

Parasitology ◽  
1973 ◽  
Vol 66 (1) ◽  
pp. 33-42 ◽  
Author(s):  
Peter W. Pappas ◽  
Clark P. Read
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Molecular Species ◽  
Basic Amino Acid ◽  
Acid Transport ◽  
Taenia Crassiceps ◽  
Acid Absorption ◽  
Straight Line ◽  
Methionine Uptake

The free pool amino acids of Taenia crassiceps metacestodes (advanced larvae) were analyzed quantitatively. In addition, the uptake of L-glutamic acid, L-proline, L-phenylalanine, L-lysine, and L-methionine was studied. Proline and glutamic acid absorption followed straight-line kinetics with respect to substrate concentration, and were not inhibited by their own molecular species. Lysine, phenylalanine and methionine were found to enter larvae by a combination of diffusion and mediated processes. Lysine absorption was inhibited only by lysine, arginine and ornithine. Phenylalanine and methionine uptake was not inhibited by lysine or arginine, but was inhibited by several other amino acids. The data suggested the presence of a basic amino acid transport locus and two distinct transport loci for methionine absorption. In addition, both immature and advanced larvae were found to be impermeable to [14C]inulin (M.W. ca. 5000). These results are discussed and compared with the results of earlier investigations of protein and amino acid absorption by T. crassiceps larvae.

scholarly journals Presence of histones in Aspergillus nidulans.

1976 ◽  
Vol 68 (3) ◽  
pp. 430-439 ◽  
Author(s):  
R A Felden ◽  
M M Sanders ◽  
N R Morris
Keyword(s):  
Molecular Weight ◽  
Acetic Acid ◽  
Amino Acid ◽  
Aspergillus Nidulans ◽  
Amino Acid Analysis ◽  
Gel Chromatography ◽  
Mobility Patterns ◽  
Net Charge ◽  
Basic Proteins ◽  
Calf Thymus

Five major histone proteins have been extracted from chromatin isolated from purified nuclei of the fungus, Aspergillus nidulans. These proteins had chromatographic properties which were similar to reference calf thymus histones and were purified to electrophoretic homegeneity by gel chromatography of Bio-Gel P10, Bio-Gel P60, and Sephadex G-100. Electrophoresis of these proteins in three different systems (urea-starch, urea-acetic acid polyacrylamide, and discontinuous SDS polyacrylamide) showed that the A. nidulans histones H3 and H4 were nearly identical to calf thymus H3 and H4 with respect to net charge and molecular weight criteria, whereas the fungal histones H1, H2a and H2b were similar but not identical to the corresponding calf thymus histones. Amino acid analysis of A. nidulans histones H2a, H2b, and H4 showed them to be closely related to the homologous calf thymus histones. The mobility patterns of A. nidulans ribosomal basic proteins in three different electrophoretic systems were distinctly different from those of the fungal histones.

ZONE ELECTROPHORESIS OF CALF THYMUS HISTONE IN STARCH GEL

1960 ◽  
Vol 38 (4) ◽  
pp. 355-363 ◽  
Author(s):  
J. M. Neelin ◽  
E. M. Neelin
Keyword(s):  
Amino Acids ◽  
Gel Electrophoresis ◽  
Low Ph ◽  
Acid Extraction ◽  
Starch Gel Electrophoresis ◽  
Calf Thymus ◽  
Zone Electrophoresis ◽  
Starch Gel ◽  
Terminal Amino

A total of 19 zones were detected by starch gel electrophoresis of calf thymus histone in buffers of 0.02 μ below pH 5.0. Of these, 18 were evident at pH 4.9 (acetate) and 15 at pH 3.9 (formate). Above pH 5.0, aggregation interfered with resolution, but by adding 4 M urea to the gel sufficient resolution was obtained between pH 4.4 and 8.7 to distinguish a total of 22 zones. Of this total, three fast components were present only occasionally in trace amounts, and three others were resolved from the immobile aggregated histone at low pH only. At least 16 zones appeared to be native histone components. Acid extraction of the histone did not appear to cause degradation since no new N-terminal amino acids were generated by this step. Two different methods of preparation produced histone extracts with essentially the same electrophoretic properties.

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