scholarly journals A MELTING POINT FOR THE BIREFRINGENT COMPONENT OF MUSCLE

1966 ◽  
Vol 30 (3) ◽  
pp. 453-464 ◽  
Author(s):  
John F. Aronson
Keyword(s):  
Transition Temperature ◽  
Ionic Strength ◽  
Striated Muscle ◽  
Species Difference ◽  
Psoas Muscle ◽  
Rabbit Muscle ◽  
Large Decrease ◽  
Factors Affecting ◽  
Wide Ph Range ◽  
The Stability

The A filament of the striated muscle sarcomere is an ordered aggregate of one or a few species of proteins. Ordering of these filaments into a parallel array is the basis of birefringence in the A region, and loss of birefringence is therefore a measure of decreased order. Heating caused a large decrease in the birefringence of glycerinated rabbit psoas muscle fibers over a narrow temperature range (∼3°C) and a large decrease in both the birefringence and optical density of the A region of Drosophila melanogaster fibrils. These changes were interpreted as a loss of A filament structure and were used to define a transition temperature (Ttr) as a measure of the stability of the A region. Since the transition temperature was sensitive to pH, ionic strength, and urea, solvent conditions which often affect protein structure, it is an experimentally useful indicator for factors affecting the structure of the A filament. Fibers from glycerinated frog muscle were less stable over a wide pH range than fibers from glycerinated rabbit muscle, a fact which demonstrates a species difference in structure. Glycerinated rabbit fibrils heated to 70°C shortened to about 40% of their initial length. The extent of shortening was not correlated with the loss of birefringence, and phase-contrast microscopy showed that this shortening occurred in the I region as well as in the A region. This response may be useful for studying the I filament and actin in much the same way that the decrease in birefringence was used for studying the A filament and myosin. The observations presented show that some properties of muscle proteins can be studied essentially in situ without the necessity of first dispersing the structure in solutions of high or low ionic strength.

Factors affecting the stability of chitosan/tripolyphosphate micro- and nanogels: resolving the opposing findings

2015 ◽  
Vol 3 (29) ◽  
pp. 5957-5970 ◽  
Author(s):  
Yan Huang ◽  
Yuhang Cai ◽  
Yakov Lapitsky
Keyword(s):  
Ionic Strength ◽  
Particle Concentration ◽  
Factors Affecting ◽  
The Stability

The stability of submicron chitosan/tripolyphosphate particles depends on the chitosan type, pH, ionic strength and particle concentration.

Analysis of the Factors Affecting the Realization of Lambda Transition Temperature of 4He

2011 ◽  
Vol 18 (1) ◽  
pp. 13-24 ◽  
Author(s):  
L. Yin ◽  
P. Lin ◽  
J. Zhao ◽  
X. Qi
Keyword(s):  
Transition Temperature ◽  
Heat Flow ◽  
Depression Effect ◽  
Resistance Thermometer ◽  
Factors Affecting ◽  
Heat Flows ◽  
Flow Through ◽  
Lambda Transition ◽  
The Stability ◽  
Temperature Plateau

Analysis of the Factors Affecting the Realization of Lambda Transition Temperature of 4He Owing to the dramatic change in the thermal conductivity of 4He when its temperature crosses the transition of superfluid (HeI) and normalfluid (HeII), a sealed-cell with a capillary is used to realize the lambda transition temperature, Tλ. A small heat flow is controlled through the capillary of the sealed-cell so as to realize the coexistence of HeI and HeII and maintain the stay of HeI/HeII interface in the capillary. A stable and flat lambda transition temperature "plateau" is obtained. Because there is a depression effect of Tλ caused by the heat flow through the capillary, a series of heat flows and several temperature plateaus are made and an extrapolation is applied to determine Tλ with zero heat flow. A rhodium-iron resistance thermometer with series number A34 (RIRT A34) has been used in 24 Tλ -realization experiments to derive Tλ with a standard deviation of 0.022mK, which proves the stability and reproducibility of Tλ.

Thermodynamic Studies of the Core Histones:  pH and Ionic Strength Effects on the Stability of the (H3−H4)/(H3−H4)2System†

Biochemistry ◽  
1996 ◽  
Vol 35 (6) ◽  
pp. 2037-2046 ◽  
Author(s):  
Vassiliki Karantza ◽  
Ernesto Freire ◽  
Evangelos N. Moudrianakis
Keyword(s):  
Ionic Strength ◽  
Thermodynamic Studies ◽  
The Core ◽  
Core Histones ◽  
The Stability

scholarly journals Stability Studies of Transition Metal Chelates of 5-Bromosalicylidene-4-methoxyaniline andSalicylidene-2,3-dimethylaniline as Ligands

2011 ◽  
Vol 8 (4) ◽  
pp. 1911-1915
Author(s):  
N. G. Nadkarni ◽  
K. V. Mangaonkar
Keyword(s):  
Ionic Strength ◽  
Transition Metal ◽  
Stability Constants ◽  
Metal Chelates ◽  
Ternary Complexes ◽  
Water Medium ◽  
Stability Studies ◽  
Binary And Ternary Complexes ◽  
Transition Metal Chelates ◽  
The Stability

Binary and ternary complexes of the type M-Y and M-X-Y [M = Mn(II), Ni(II), Cu(II) and Zn(II); X = 5-bromosalicylidene-4-methoxyaniline and Y = salicylidene-2,3-dimethylaniline] have been examined pH-metrically at 27±0.5°C and at constant ionic strength, μ = 0.1 M (KCl) in 75 : 25(v/v) 1,4-dioxne-water medium. The stability constants for binary (M-Y) and ternary (M-X-Y) systems were calculated.

CRITICAL REVIEW OF EMULSION STABILITY AND CHARACTERIZATION TECHNIQUES IN OIL PROCESSING

2021 ◽  
pp. 1-36
Author(s):  
Vahideh Angardi ◽  
Ali Ettehadi ◽  
Özgün Yücel
Keyword(s):  
Separation Efficiency ◽  
Petroleum Industry ◽  
Cost Effective ◽  
Downstream Processing ◽  
Physical Factors ◽  
Comprehensive Review ◽  
Factors Affecting ◽  
Mathematical Explanations ◽  
The Stability ◽  
The Right

Abstract Effective separation of water and oil dispersions is considered a critical step in the determination of technical and economic success in the petroleum industry over the years. Moreover, a deeper understanding of the emulsification process and different affected parameters is essential for cost-effective oil production, transportation, and downstream processing. Numerous studies conducted on the concept of dispersion characterization indicate the importance of this concept, which deserves attention by the scientific community. Therefore, a comprehensive review study with critical analysis on significant concepts will help readers follow them easily. This study is a comprehensive review of the concept of dispersion characterization and conducted studies recently published. The main purposes of this review are to 1) Highlight flaws, 2) Outline gaps and weaknesses, 3) Address conflicts, 4) Prevent duplication of effort, 5) List factors affecting dispersion. It was found that the separation efficiency and stability of dispersions are affected by different chemical and physical factors. Factors affecting the stability of the emulsions have been studied in detail and will help to look for the right action to ensure stable emulsions. In addition, methods of ensuring stability, especially coalescence are highlighted, and coalescence mathematical explanations of phenomena are presented.

scholarly journals Influence of the Al content on the phase transformations in Cu-Al-Ag alloys

2003 ◽  
Vol 28 (1) ◽  
pp. 33-38 ◽  
Author(s):  
A. T. Adorno ◽  
A. V. Benedetti ◽  
R. A. G. da Silva ◽  
M. Blanco
Keyword(s):  
Thermal Analysis ◽  
Differential Thermal Analysis ◽  
Transition Temperature ◽  
Phase Transformations ◽  
Decomposition Reaction ◽  
Phase Decomposition ◽  
Stability Range ◽  
X Ray ◽  
Al Content ◽  
The Stability

The influence of the Al content on the phase transformations in Cu-Al-Ag alloys was studied by classical differential thermal analysis (DTA), optical microscopy (OM) and X-ray diffractometry (XRD). The results indicated that the increase in the Al content and the presence of Ag decrease the rate of the <FONT FACE=Symbol>b</font>1 phase decomposition reaction and contribute for the raise of this transition temperature, thus decreasing the stability range of the perlitic phase resulted from the b1 decomposition reaction.

Factors affecting the amplitude of the τ angle in proteins: a revisitation

2017 ◽  
Vol 73 (7) ◽  
pp. 618-625 ◽  
Author(s):  
Nicole Balasco ◽  
Luciana Esposito ◽  
Luigi Vitagliano
Keyword(s):  
Protein Structures ◽  
Factors Affecting ◽  
X Ray ◽  
Backbone Conformation ◽  
Potential Factors ◽  
The Stability ◽  
Major Factors ◽  
The Impact ◽  
Open Issues

The protein folded state is the result of the fine balance of a variety of different forces. Even minor structural perturbations may have a significant impact on the stability of these macromolecules. Studies carried out in recent decades have led to the convergent view that proteins are endowed with a flexible spine. One of the open issues related to protein local backbone geometry is the identification of the factors that influence the amplitude of the τ (N—Cα—C) angle. Here, statistical analyses performed on an updated ensemble of X-ray protein structures by dissecting the contribution of the major factors that can potentially influence the local backbone geometry of proteins are reported. The data clearly indicate that the local backbone conformation has a prominent impact on the modulation of the τ angle. Therefore, a proper assessment of the impact of the other potential factors can only be appropriately evaluated when small (φ, ψ) regions are considered. Here, it is shown that when the contribution of the backbone conformation is removed by considering small (φ, ψ) areas, an impact of secondary structure, as defined byDSSP, and/or the residue type on τ is still detectable, although to a limited extent. Indeed, distinct τ-value distributions are detected for Pro/Gly and β-branched (Ile/Val) residues. The key role of the local backbone conformation highlighted here supports the use of variable local backbone geometry in protein refinement protocols.

scholarly journals QUANTITATIVE AND HISTOCHEMICAL STUDIES ON THE DESORPTION AND READSORPTION OF ALDOLASE IN CROSS-STRIATED MUSCLE

1969 ◽  
Vol 17 (5) ◽  
pp. 314-320 ◽  
Author(s):  
H. ARNOLD ◽  
J. NOLTE ◽  
D. PETTE
Keyword(s):  
Enzyme Activity ◽  
Actin Filaments ◽  
Phosphate Buffer ◽  
Striated Muscle ◽  
Psoas Muscle ◽  
Histochemical Staining ◽  
Intracellular Location ◽  
Successive Extraction ◽  
Complete Extraction

Complete extraction of aldolase from minced rabbit psoas muscle was achieved by successive extraction steps in 0.1 M phosphate buffer. Aldolase was then readsorbed quantitatively to the depleted myofibrils. Extraction, readsorption and a final redsorption of the enzyme were followed quantitatively by enzyme activity determinations and qualitatively by histochemical staining of aldolase. The intracellular location of the readsorbed enzyme was found to be identical with that of aldolase in native muscle. In both cases, aldolase was localized within the isotropic bands. These results as well as the previously demonstrated binding of the enzyme to F-actin suggest that aldolase is located within the interfilamentary sarcoplasm of the isotropic bands and is probably also bound in vivo to the actin filaments.

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