Amino acid composition of sperm histones in the house cricket Acheta domesticus

1976 ◽  
Vol 54 (1) ◽  
pp. 56-61 ◽  
Author(s):  
Dominick Pallotta ◽  
Anne Tessier

Histones were isolated from late spermatids and spermatozoa of the house cricket Acheta domesticus, and the individual histone fractions were separated by electrophoresis on polyacrylamide–urea gels. The stained gels were cut so as to isolate the different histone fractions, and the amino acid compositions were determined using the technique of Houston (Houston, L. L.: Anal. Biochem. 44, 81–88 (1971)). Five of the histones had amino acid compositions resembling those for the histones of calf thymus and were thus identified as fractions F1, F3, F2a2, F2b, and F2a1. Another protein (SH) located exclusively in the late spermatids and spermatozoa was found to be basic and histone-like. It is a protein containing relatively high amounts of arginine (12.6%) and low amounts of lysine (7.6%), and, as a result, it has a low ratio of lysine–arginine (0.6). Other noteworthy features are its high contents of serine, glutamic acid, and glycine. It is an arginine rich histone and in this regard resembles other such proteins, but it does contain unique features which distinguish it from all previously described histones.

1951 ◽  
Vol 34 (4) ◽  
pp. 439-450 ◽  
Author(s):  
Marie M. Daly ◽  
A. E. Mirsky ◽  
Hans Ris

Some of the properties and the amino acid compositions of the histones of calf thymus, calf liver, fowl erythrocytes, and of a protamine-like material isolated from rooster sperm were described. The amino acid compositions of the histones were rather similar except that no methionine was found in the fowl erythrocyte histone. In the fowl, histones are found in the somatic chromosomes and protamines are found in the sperm chromosomes. This shows that great variations in chromosome composition can exist in an organism. Histone is digested by pepsin both when isolated and when in the chromosome.


1985 ◽  
Vol 54 (2) ◽  
pp. 483-492 ◽  
Author(s):  
H. A. Greife ◽  
J. A. Rooke ◽  
D. G. Armstrong

1. In a 4 x 4 Latin square experiment four cows were given, twice daily, diets consisting of (g/kg dry matter (DM)) 500 barley, 400 grass silage and 100 soya-bean meal. The diets were given at either 1.15 (L) or 2.3 (H) times maintenance energy requirements and the soya-bean meal was either untreated (U) or formaldehyde (HCH0)-treated (T).2. The passage of digesta to the duodenum was estimated using chromic oxide as a flow marker;35S was used to estimate the amount of microbial protein entering the small intestine. A microbial fraction was prepared by differential centrifugation from duodenal digesta. Samples of bacteria and of protozoa from rumen digesta were also prepared.3. The total amino acid contents of feedingstuffs, duodenal digesta, duodenal microbial material, rumen bacteria and rumen protozoa were determined by ion-exchange chromatography. The D-alanine and D-glutamic acid contents of the samples were determined by gas–liquid chromatography.4. The quantity of each amino acid entering the small intestine was significantly (P < 0,001) increased by increasing DM intake and tended to be increased by formaldehyde-treatment of the soya-bean meal. There were net losses of all amino acids across the forestomachs except for lysine, methione, o-alanine and D-glutamic acid for which there were net gains.5. There were significant (P < 0.05) differences in amino acid composition between rumen bacteria and duodenal microbial material; differences in amino acid composition between rumen bacteria and rumen protozoa were also observed.6. D-Alanine and D-glutamic acid were present in the silage but not in the barley or either of the soya-bean meals. All samples of microbes and digesta contained D-alanine and D-glutamic acid.7. The use of D-ahine and D-glUtamiC acid as markers for microbial nitrogen entering the small intestine was assessed. Estimates of the quantities of microbial N entering the small intestine based on the D-alanine or D-glutamic acid contents of rumen bacteria or duodenal microbes were significantly higher than those determined using 35S as a marker.


1970 ◽  
Vol 119 (2) ◽  
pp. 165-170 ◽  
Author(s):  
Laxman S. Desai ◽  
George E. Foley

Histones F2al extracted from normal and neoplastic cells possess similar amino acid compositions. Tryptic and chymotryptic peptides of the F2al histones have identical chromato-electrophoretic RF values. It is concluded that histones F2al from various sources have similar overall structures. The observed differences in the ratios of ∈-N-monomethyl- and di-∈-N-methyl-lysine in the histones from normal and neoplastic cells may be of significance with respect to gene regulation.


2019 ◽  
Vol 20 (20) ◽  
pp. 5136 ◽  
Author(s):  
Mentes ◽  
Magyar ◽  
Fichó ◽  
Simon

Several intrinsically disordered proteins (IDPs) are capable to adopt stable structures without interacting with a folded partner. When the folding of all interacting partners happens at the same time, coupled with the interaction in a synergistic manner, the process is called Mutual Synergistic Folding (MSF). These complexes represent a discrete subset of IDPs. Recently, we collected information on their complexes and created the MFIB (Mutual Folding Induced by Binding) database. In a previous study, we compared homodimeric MSF complexes with homodimeric and monomeric globular proteins with similar amino acid sequence lengths. We concluded that MSF homodimers, compared to globular homodimeric proteins, have a greater solvent accessible main-chain surface area on the contact surface of the subunits, which becomes buried during dimerization. The main driving force of the folding is the mutual shielding of the water-accessible backbones, but the formation of further intermolecular interactions can also be relevant. In this paper, we will report analyses of heterodimeric MSF complexes. Our results indicate that the amino acid composition of the heterodimeric MSF monomer subunits slightly diverges from globular monomer proteins, while after dimerization, the amino acid composition of the overall MSF complexes becomes more similar to overall amino acid compositions of globular complexes. We found that inter-subunit interactions are strengthened, and additionally to the shielding of the solvent accessible backbone, other factors might play an important role in the stabilization of the heterodimeric structures, likewise energy gain resulting from the interaction of the two subunits with different amino acid compositions. We suggest that the shielding of the β-sheet backbones and the formation of a buried structural core along with the general strengthening of inter-subunit interactions together could be the driving forces of MSF protein structural ordering upon dimerization.


1968 ◽  
Vol 107 (6) ◽  
pp. 745-751 ◽  
Author(s):  
G. van Vliet ◽  
T. H. J. Huisman ◽  
G. A. Dasher ◽  
W. H. Moretz ◽  
A. M. Dozy ◽  
...  

1. Two haemoglobin types, haemoglobins Amm-C and Amm-B, were observed in five Barbary sheep (Ammotragus lervia). One animal was homozygous for haemoglobin Amm-C, a second was homozygous for haemoglobin Amm-B, and three were heterozygous for both. 2. Amino acid analyses of the globin from haemoglobin Amm-B showed that this type was related to, but not identical with, haemoglobin B of the domestic sheep. 3. The β-chain of haemoglobin Amm-C was found to be composed of 141 amino acid residues. Its amino acid composition differed from that of the βC-chain of the anaemic domestic sheep in at least 14 residues. The Amm-βC-chain contained one isoleucyl residue. 4. The amino acid compositions of tryptic peptides T-1, T-2, T-13 and T-14 of the Amm-βC-chain were similar to those of the sheep βC-chain. Peptides T-3, T-4, T-6, T-7, T-8, T-11 and T-15 were the same as the corresponding peptides of the sheep βA- and βC-chains. Peptide T-5 and to a smaller extent peptide T-9 resembled the corresponding peptides of the sheep βA-chain, and peptide T-10 was identical with peptide γT-10 of sheep haemoglobin F. Peptide T-12 was not recovered. 5. The results of these investigations were interpreted as being indicative that the structural Amm-βC-gene is closely related to the βC-gene of sheep, from which through domestication the present domestic sheep originated.


Author(s):  
A. I. Fedosov ◽  
V. S. Kyslychenko ◽  
O. M. Novosel

Introduction. Plant amino acids have an important impact on functioning of various systems and organs of human body. In addition, they possess a wide range of pharmacotherapeutic properties, improve the digestion and potentiate the activity of biologically active compounds present in plants. Thus, the search of plant species that contain a large complex of plant amino acids and are used as food is of current interest. Garlic (Allium sativum L.) from Alliaceae family is one of such plants, and has been used since ancient times for the treatment of various disorders.The aim of the study – to determine the composition and quantitative content of free and bound amino acids of garlic bulbs and leaves.Research methods. The amino acid composition was determined using the high-performance liquid chromatography (HPLC) method.Results and Discussion. 16 amino acids were detected in garlic bulbs as a result of the experiment. Arginine (3.04 %) and proline (1.56 %) were found to be accumulated infree state, while glutamic acid (10.59 %), aspartic acid (6.06 %) and arginine (5.94 %) prevailed in bound state. 15 free and 16 bound amino acids were identified and quantified in garlic leaves. Glutamic acid (2.11 %), leucine (1.79 %), valine (1.77 %), isoleucine (1.52 %), treonine and phenylalanine (1.44 %) dominated infree state, and glutamic acid (28.49 %), aspartic acid (12.90 %) and leucine (7.61 %) prevailed in bound state. Methionine was found only in bound state in garlic leaves.Conclusions. The amino acid composition of garlic bulbs and leaves was studied using the HPLC method. 16 amino acids in both free and bound state were detected and their content was determined in garlic bulbs, while in garlic leaves – 15 free and 16 bound amino acids. The results of the experiment showed that methionine is present only in bound state in garlic leaves.


1978 ◽  
Vol 58 (2) ◽  
pp. 237-249 ◽  
Author(s):  
F. J. SOWDEN ◽  
H. MORITA ◽  
M. LEVESQUE

The nitrogenous products formed by 6 N HCl hydrolysis of a variety of peats including a cultivated mesic profile, a virgin humic profile, a sedge, a woody and a sphagnum fibric peat were studied. Peat fractions separated according to particle size, woody and herbaceous materials isolated from a peat sample, and Typha and Carex plants growing on peat soils were also analyzed. Of the two profiles examined, the cultivated mesic peat showed significant quantitative changes in the content of individual amino acids throughout the profile. Also the amino sugar and amino acid N increased to a maximum, then decreased. On the other hand, the virgin humic peat profile exhibited random variations in the content of the individual amino acids and in the amount of amino acid N. Of the other peats examined, the fibric sphagnum had the highest percentage of amino acid N. Among the separates, the 100- to 200-mesh material had the highest proportion of amino acid N. The amino acid composition of the plant remains from the peat was similar to that of the peat from which it was isolated. The amino acid composition of the Typha and Carex plants was different from that of peat in that 75% of their total N content could be accounted for on the basis of amino acid, amide and amino sugar N. The amounts of hydroxyproline and the amino sugars in peats vary more than that of the amino compounds. In contrast to inorganic soils, which tend to have a similar amino acid composition, these limited data suggest that the amino acid and amino sugar contents of peats may be characteristic of individual bogs.


1981 ◽  
Vol 8 (2) ◽  
pp. 131-133 ◽  
Author(s):  
David C. H. Hsi ◽  
Clyde T. Young ◽  
Melchor Ortiz

Abstract Two Valencia peanut (Arachis hypogaea L.) cultivars, New Mexico Valencia A and New Mexico Valencia C, were grown at Arch and Los Lunas, N. M. All peanuts were grown under either sprinkler or furrow irrigation. Samples were obtained following harvest, hydrolyzed and analyzed in Raleigh, N. C. for amino acid content. With samples from Arch, no variety by planting date effects were noted for amino acid composition. With samples from Los Lunas, however, significant variety by planting date effects were noted for glutamic acid, glycine, methionine, isoleucine, and leucine. Planting date effects were found only for glycine at the Los Lunas location and phenylalanine at both locations. Significant variety differences were found for methionine, tyrosine, phenylalanine, and lysine at the Arch location and for glycine, methionine, phenylalanine, and lysine at the Los Lunas location. A significant year effect, although small, was noted for about half of the amino acids (aspartic acid, serine, glutamic acid, proline, glycine, tyrosine, phenylalanine, arginine, and the sum of all amino acids) studied at the Arch location. Data at Los Lunas were observed only during the second year. The amino acid content agrees closely with that previously reported for other types of peanuts except for a 100% higher level of cystine found in this study.


1975 ◽  
Vol 53 (5) ◽  
pp. 561-564 ◽  
Author(s):  
Keith Scott ◽  
Burt Zerner

The amino acid compositions of the carboxylesterases from chicken, horse, ox, sheep, and pig livers are reported and compared. As would be expected for this homologous series, the compositions show a general similarity. However, there are some significant differences, but the degree to which particular pairs of enzymes differ is consistent with the evolutionary history of the species from which they were isolated.


1972 ◽  
Vol 78 (2) ◽  
pp. 265-273 ◽  
Author(s):  
D. B. Smith

SUMMARYThe amino acid composition of barley grain was studied during the maturation of the grain and during germination of the mature grain. Samples of the variety Proctor, grown at two nitrogen levels in each of the years 1969 and 1970, were analysed together with one sample of Sultan grown in 1970. It was found that during maturation the proportions of glutamic acid and proline increased and that the levels of these amino acids were highest in those samples with the highest total protein content. During ripening the proportions of lysine, alanine, aspartic acid, threonine and glycine decreased. On germination the proportions of glutamic acid and proline rapidly decreased whilst aspartic acid, lysine, alanine and glycine increased.The nutritive value of ripe barley grain is limited by its low lysine content. Whilst the germination process increases the level of lysine it is suggested that this does not increase the nutritional value of the grain due to the low level of cystine in the germinated grain.


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