scholarly journals Homologies in amino acid composition and structure of histone F2al isolated from human leukaemic cells

1970 ◽  
Vol 119 (2) ◽  
pp. 165-170 ◽  
Author(s):  
Laxman S. Desai ◽  
George E. Foley
Keyword(s):  
Gene Regulation ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Neoplastic Cells ◽  
Amino Acid Compositions ◽  
Composition And Structure ◽  
Leukaemic Cells ◽  
Rf Values ◽  
Similar Amino Acid

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.

scholarly journals Analysis of Heterodimeric “Mutual Synergistic Folding”-Complexes

2019 ◽  
Vol 20 (20) ◽  
pp. 5136 ◽  
Author(s):  
Mentes ◽  
Magyar ◽  
Fichó ◽  
Simon
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Intrinsically Disordered Proteins ◽  
Driving Forces ◽  
Disordered Proteins ◽  
Subunit Interactions ◽  
Amino Acid Compositions ◽  
Intrinsically Disordered ◽  
Β Sheet

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.

scholarly journals Studies of haemoglobin types in barbary sheep (Ammotragus lervia)

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 ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Domestic Sheep ◽  
Amino Acid Residues ◽  
Amino Acid Compositions ◽  
Ammotragus Lervia ◽  
Peptide T ◽  
Barbary Sheep ◽  
Β Chain

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.

Carboxylesterases (EC 3.1.1). Amino Acid Composition of Liver Carboxylesterases

1975 ◽  
Vol 53 (5) ◽  
pp. 561-564 ◽  
Author(s):  
Keith Scott ◽  
Burt Zerner
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Homologous Series ◽  
Evolutionary History ◽  
Amino Acid Compositions ◽  
General Similarity ◽  
History Of

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.

The isolation and properties of 1·6 S γ -histone from calf thymocytes

1958 ◽  
Vol 149 (934) ◽  
pp. 36-41 ◽  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Physicochemical Properties ◽  
Amino Acid Composition ◽  
High Molecular Weight ◽  
Acid Composition ◽  
The Other ◽  
Amino Acid Compositions

The isolation of 1·6 S γ -histone is described, its amino-acid composition recorded and an account given of some of its physicochemical properties. Its molecular weight has been calculated from sedimentation velocities to be 74000 in its unaggregated condition. It thus represents a second histone of high molecular weight present in the nuclei of calf thymocytes. Both β and 1·6 S γ -histone are distinguished from the other four components in their ability to undergo aggregation. The γ -histone, however, does not aggregate so readily or so extensively as does β -histone. These two histones are also clearly distinguished by their amino-acid compositions.

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
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Acheta Domesticus ◽  
House Cricket ◽  
Amino Acid Compositions ◽  
Calf Thymus ◽  
The Individual

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.

scholarly journals THE AMINO ACID COMPOSITION AND SOME PROPERTIES OF HISTONES

1951 ◽  
Vol 34 (4) ◽  
pp. 439-450 ◽  
Author(s):  
Marie M. Daly ◽  
A. E. Mirsky ◽  
Hans Ris
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Amino Acid Compositions ◽  
Calf Thymus ◽  
Sperm Chromosomes

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.

scholarly journals The in vitro determination of the protein quality of rumen microorganisms of cows on urea-rich feed

1979 ◽  
Vol 51 (1) ◽  
pp. 68-78
Author(s):  
Eeva-Liisa Syväoja ◽  
Matti Kreula
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Protein Quality ◽  
Diaminopimelic Acid ◽  
In Vitro Digestibility ◽  
Amino Acid Compositions

The amino acid composition, essential amino acid index (EAA-I), pepsin-pancreatin in vitro digestibility and pepsin-pancreatin-digest-residue-index (PPDR-I) of the rumen bacterial and protozoal protein of cows fed urea and ammonium salts as their sole source of nitrogen (0-cows) or as a partial source (ULP-cows), and of cows on normal protein-rich feed (NorP-cows), were determined. The amino acid compositions of the rumen bacteria showed very slight changes even though the diets were very different. The amino acid compositions of the pure bacterial strains isolated from the rumina differed slightly. The amino acid compositions of the rumen protozoa of the ULP- and NorP-cows differed only with respect to isoleucine and tyrosine. Protozoa could be found only occasionally in the rumen of the 0-cow, there being only two species. Their nutritional significance was obviously very small. When the nutritional quality of the microbial protein was studied on the basis of its amino acid composition it was found that the EAA-I of bacteria did not differ significantly. Neither did the EAA-I of protozoa differ. The pepsin-pancreatin in vitro digestibility of protozoa was higher on all the feeds than that of bacteria. The rumen bacterial in vitro digestibility with 0-cows differed from that of the ULP-samples but not from that of the NorP-samples. The digestibility of single amino acids, With the exception of diaminopimelic acid, glycine and alanine, did not differ from the digestibility of the total amino acids. The much larger number of bacteria in the rumen of 0-cows compared with those of ULP- and NorP-cows compensates in this way for the lower digestibility of bacterial protein in 0-cows. The PPDR-I of both bacteria and protozoa were well correlated with the in vitro digestibility.

scholarly journals The purification and amino acid composition of human uterus collagens, rheumatoid-arthritis-nodule collagen and ox tendon collagen

1968 ◽  
Vol 106 (3) ◽  
pp. 749-757 ◽  
Author(s):  
J J Harding ◽  
J. M. Wesley
Keyword(s):  
Rheumatoid Arthritis ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Post Partum ◽  
Human Uterus ◽  
Amino Acid Compositions ◽  
Organic Extractants ◽  
Post Menopausal ◽  
Tendon Collagen

Collagens and gelatins were isolated from human post-menopausal uterus, puerperal (post-partum) uterus, rheumatoid-arthritis-nodule and ox tendon. Different means of purifying collagen were studied and a method was devised that enables highly purified collagen to be obtained, even from the uterus. This method involves the use of a number of aqueous and organic extractants as well as digestion with elastase to eliminate elastin. The purity of the collagen preparations was assessed and they were used to study the amino acid composition of collagen. The amino acid compositions of all the collagens studied were similar to those of human bone and tendon collagen, but certain small differences were noted and are discussed. The soluble collagen extracted from some of the tissues was also studied.

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