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.

scholarly journals Molecular weight, amino acid composition and physicochemical properties of the exocellular dd-carboxypeptidase–transpeptidase of Streptomyces R39

1974 ◽  
Vol 143 (1) ◽  
pp. 233-240 ◽  
Author(s):  
Jean-Marie Frère ◽  
Ramon Moreno ◽  
Jean-Marie Ghuysen ◽  
Harold R. Perkins ◽  
Louis Dierickx ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Physicochemical Properties ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Polypeptide Chain

The exocellular dd-carboxypeptidase–transpeptidase from Streptomyces R39 was purified to protein homogeneity and in milligram amounts. The isolated enzyme consisted of one polypeptide chain of molecular weight about 53300. Its amino acid composition and several physicochemical properties were determined and compared with those of the exo-cellular dd-carboxypeptidase–transpeptidase from Streptomyces R61.

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  Quality of rabbit meat and phyto-additives

2010 ◽  
Vol 28 (No. 3) ◽  
pp. 161-167 ◽  
Author(s):  
M.P. Simonová ◽  
Ľ. Chrastinová ◽  
J. Mojto ◽  
A. Lauková ◽  
R. Szábová ◽  
...  
Keyword(s):  
Amino Acid ◽  
Physicochemical Properties ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Plant Extracts ◽  
Good Health ◽  
Good Alternative ◽  
Health State ◽  
Rabbit Meat

The consumption of healthy and nutritive food (rich in proteins and low in cholesterol and lipid contents) is a preferred factor with the contemporary consumers. In addition, natural alternatives are requested to replace the additives used up to now but recently banned. To reach the above given condition, phyto-additives represent a good alternative. The aim of this study was to examine the physicochemical properties and amino acid composition of rabbit meat after the enrichment of rabbit diet with oregano, sage, and Eleutherococcus senticosus extracts, and to make a comparison with the commercial product XTRACT and control samples (without plant extracts). The addition of oregano and sage extracts as well as El. senticosus in the rabbit diet positively influenced the physicochemical properties of rabbit meat by increasing its energy value (P < 0.05 – sage). Supplementing rabbits feed with oregano and sage extracts led to an improvement on the amino acid composition (P < 0.01; P < 0.001 – serine). These findings are also supported by the good health state of rabbits. Outgoing from these results, the diet enriched with the plant extracts is beneficial for the health state of rabbits involving the nutritional quality of rabbit meat in connection with consumers.

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.

Sign in / Sign up

Export Citation Format

Share Document