Effect of artificial gravity in space flight on the content of water-soluble proteins in nerve tissue structures

1978 ◽  
Vol 86 (4) ◽  
pp. 1308-1311 ◽  
Author(s):  
A. V. Gorbunova ◽  
V. V. Portugalov
Keyword(s):  
Space Flight ◽  
Soluble Proteins ◽  
Water Soluble ◽  
Artificial Gravity ◽  
Nerve Tissue ◽  
Tissue Structures

The cellular basis of corneal transparency: evidence for ‘corneal crystallins’

1999 ◽  
Vol 112 (5) ◽  
pp. 613-622 ◽  
Author(s):  
J.V. Jester ◽  
T. Moller-Pedersen ◽  
J. Huang ◽  
C.M. Sax ◽  
W.T. Kays ◽  
...  
Keyword(s):  
Cellular Level ◽  
Soluble Proteins ◽  
Water Soluble ◽  
Corneal Tissue ◽  
Corneal Epithelial Cells ◽  
Corneal Epithelial ◽  
Corneal Transparency ◽  
Scattering Measurements ◽  
Class 1

In vivo corneal light scattering measurements using a novel confocal microscope demonstrated greatly increased backscatter from corneal stromal fibrocytes (keratocytes) in opaque compared to transparent corneal tissue in both humans and rabbits. Additionally, two water-soluble proteins, transketolase (TKT) and aldehyde dehydrogenase class 1 (ALDH1), isolated from rabbit keratocytes showed unexpectedly abundant expression (approximately 30% of the soluble protein) in transparent corneas and markedly reduced levels in opaque scleral fibroblasts or keratocytes from hazy, freeze injured regions of the cornea. Together these data suggest that the relatively high expressions of TKT and ALDH1 contribute to corneal transparency in the rabbit at the cellular level, reminiscent of enzyme-crystallins in the lens. We also note that ALDH1 accumulates in the rabbit corneal epithelial cells, rather than ALDH3 as seen in other mammals, consistent with the taxon-specificity observed among lens enzyme-crystallins. Our results suggest that corneal cells, like lens cells, may preferentially express water-soluble proteins, often enzymes, for controlling their optical properties.

Selective Transport of Water-Soluble Proteins from Aqueous to Ionic Liquid Phase via a Temperature-Sensitive Phase Change of These Mixtures

2012 ◽  
Vol 65 (11) ◽  
pp. 1548 ◽  
Author(s):  
Yuki Kohno ◽  
Nobuhumi Nakamura ◽  
Hiroyuki Ohno
Keyword(s):  
Phase Change ◽  
Aqueous Phase ◽  
Selective Dissolution ◽  
Selective Extraction ◽  
Soluble Proteins ◽  
Water Soluble ◽  
Temperature Sensitive ◽  
Salting Out ◽  
Key Factor ◽  
The Difference

Mixtures of some ionic liquids (ILs) and water show reversible phase change between a homogeneous mixture and phase-separated state by a small change in temperature. Some water-soluble proteins have been migrated from the aqueous to the IL phase. When tetrabutylphosphonium 2,4,6-trimethylbenzenesulfonate was used as an IL, cytochrome c (Cyt.c) was found to be extracted from the water phase to the IL phase. Conversely, both horseradish peroxidase (HRP) and azurin remained in the aqueous phase. This selective extraction was comprehended to be due to the difference in solubility of these proteins in both phases. The separated aqueous phase contained a small amount of IL, which induced the salting-out of Cyt.c. On the other hand, condensed IL phase promoted the salting-in of Cyt.c. As a result, Cyt.c was preferably dissolved in the hydrated IL phase rather than aqueous phase. In the case of HRP, there was only a salting-out profile upon increasing the concentration of IL, which induced selective dissolution of HRP in the aqueous phase. These results clearly suggest that the profile of salting-out and salting-in for proteins is the key factor to facilitate the selective extraction of proteins from aqueous to the IL phase.

scholarly journals Influence of temperature processing on the constitutive and inducible resistance of rye seedlings to chloride salinization

2021 ◽  
pp. 134-140
Author(s):  
L. A. Chudinova ◽  
◽  
D. R. Yusupov ◽  
Keyword(s):  
Growth Rate ◽  
Sodium Chloride ◽  
Protective Effect ◽  
Soluble Proteins ◽  
Final Concentration ◽  
Water Soluble ◽  
Thermal Pretreatment ◽  
Thermal Hardening ◽  
Influence Of Temperature ◽  
Inducible Synthesis

We studied the growth rate of rye seedlings, as well as the dynamics of the content of soluble proteins and proline in the shoots during their adaptation to sharp (300 mM NaCl once, exposure time 9 days) and gradual (100 mM NaCl, then 100 mM NaCl after 2 days to the final concentration of 400 mM) salinity with sodium chloride in the presence or absence of thermal hardening (+40°C, 3 h). The established dy-namics of the content of proline and soluble proteins in the shoots suggests that the formation of re-sistance to salinity is determined by the high constitutive level of proline, as well as the stress-inducible synthesis of proline and water-soluble proteins. Thermal pretreatment of the seedlings stimulated their constitutive stability to a greater extent. The detected metabolic changes are obviously related to one of the possible mechanisms of the protective effect of thermal hardening on subsequent salinization.

scholarly journals Membrane Proteins Are Dramatically Less Conserved than Water-Soluble Proteins across the Tree of Life

2016 ◽  
Vol 33 (11) ◽  
pp. 2874-2884 ◽  
Author(s):  
Victor Sojo ◽  
Christophe Dessimoz ◽  
Andrew Pomiankowski ◽  
Nick Lane
Keyword(s):  
Membrane Proteins ◽  
Soluble Proteins ◽  
Tree Of Life ◽  
Water Soluble

Emulsifying properties of water-soluble proteins extracted from the microalgae Chlorella sorokiniana and Phaeodactylum tricornutum

2019 ◽  
Vol 10 (2) ◽  
pp. 754-764 ◽  
Author(s):  
Sandra Ebert ◽  
Lutz Grossmann ◽  
Jörg Hinrichs ◽  
Jochen Weiss
Keyword(s):  
Environmental Conditions ◽  
Phaeodactylum Tricornutum ◽  
Soluble Proteins ◽  
Chlorella Sorokiniana ◽  
Water Soluble ◽  
Emulsifying Properties ◽  
New Protein

This work studies the emulsifying properties of new protein extracts of microalgae in different environmental conditions.

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