l -histidine improves water retention of heat-induced gel of chicken breast myofibrillar proteins in low ionic strength solution

2016 ◽  
Vol 51 (5) ◽  
pp. 1195-1203 ◽  
Author(s):  
Xing Chen ◽  
Yong Li ◽  
Ruiyun Zhou ◽  
Zhaiming Liu ◽  
Fengzhi Lu ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Water Retention ◽  
Chicken Breast ◽  
Myofibrillar Proteins ◽  
Low Ionic Strength

Solubility of Chicken Breast Muscle Proteins in Solutions of Low Ionic Strength

1996 ◽  
Vol 44 (2) ◽  
pp. 408-415 ◽  
Author(s):  
Ganesan Krishnamurthy ◽  
Hsin-Sui Chang ◽  
Herbert O. Hultin ◽  
Yuming Feng ◽  
Subramanian Srinivasan ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Muscle Proteins ◽  
Low Ionic Strength

Solubility of Beef and Chicken Myofibrillar Proteins in Low Ionic Strength Media

1994 ◽  
Vol 42 (4) ◽  
pp. 863-867 ◽  
Author(s):  
David W. Stanley ◽  
Ashley P. Stone ◽  
Herbert O. Hultin
Keyword(s):  
Ionic Strength ◽  
Myofibrillar Proteins ◽  
Low Ionic Strength

Improved Solubility of Carp Myofibrillar Proteins in Low Ionic Strength Medium by Glycosylation

1997 ◽  
Vol 45 (9) ◽  
pp. 3419-3422 ◽  
Author(s):  
Hiroki Saeki ◽  
Keisuke Inoue
Keyword(s):  
Ionic Strength ◽  
Myofibrillar Proteins ◽  
Low Ionic Strength ◽  
Strength Medium

Solubilization of Cod Myofibrillar Proteins at Low Ionic Strength by Sodium Pyruvate During Frozen Storage

1975 ◽  
Vol 32 (9) ◽  
pp. 1629-1632 ◽  
Author(s):  
V. D. Tran
Keyword(s):  
Ionic Strength ◽  
Protein Solubility ◽  
Frozen Storage ◽  
Myofibrillar Proteins ◽  
Sodium Pyruvate ◽  
Low Ionic Strength

The effects of adding sodium pyruvate and KCl (0–0.6 M) on protein solubility in cod homogenates were compared. KCl extracted slightly more protein than sodium pyruvate did in samples kept at 0 C for up to 5 days. In contrast, sodium pyruvate extracted more protein than did KCl in samples kept at −20 C for up to 14 days. In the presence of sodium pyruvate, changes occurred during freezing and frozen storage, which caused the myofibrillar proteins to become soluble at ionic strengths as low as 0.1.

Solubilization of myofibrillar proteins in water or low ionic strength media: Classical techniques, basic principles, and novel functionalities

2017 ◽  
Vol 57 (15) ◽  
pp. 3260-3280 ◽  
Author(s):  
Xing Chen ◽  
Ron K. Tume ◽  
Xinglian Xu ◽  
Guanghong Zhou
Keyword(s):  
Ionic Strength ◽  
Myofibrillar Proteins ◽  
Basic Principles ◽  
Low Ionic Strength

SOME PROPERTIES OF MYOFIBRILLAR PROTEINS OBTAINED FROM LOW IONIC STRENGTH EXTRACTS OF WASHED MYOFIBRILS FROM PRE- AND POST-RIGOR CHICKEN PECTORAL MUSCLE

1970 ◽  
Vol 35 (4) ◽  
pp. 464-468 ◽  
Author(s):  
TOSHIYUKI FUKAZAWA ◽  
HIROYASU NAKAI ◽  
SHIRO OHKI ◽  
TSUTOMU YASUI
Keyword(s):  
Ionic Strength ◽  
Pectoral Muscle ◽  
Myofibrillar Proteins ◽  
Low Ionic Strength

Conformational Transitions in Escherichia coli Ribosomal RNAs as Visualized by Dedicated STEM

1988 ◽  
Vol 46 ◽  
pp. 176-177
Author(s):  
J.S. Wall ◽  
V. Maridiyan ◽  
S. Tumminia ◽  
J. Hairifeld ◽  
M. Boublik
Keyword(s):  
Ionic Strength ◽  
Three Dimensional ◽  
Conformational Transitions ◽  
Dark Field ◽  
Dimensional Structure ◽  
Ribosomal Rnas ◽  
Field Mode ◽  
Freeze Dried ◽  
High Resolution Images ◽  
Low Ionic Strength

The high contrast in the dark-field mode of dedicated STEM, specimen deposition by the wet film technique and low radiation dose (1 e/Å2) at -160°C make it possible to obtain high resolution images of unstained freeze-dried macromolecules with minimal structural distortion. Since the image intensity is directly related to the local projected mass of the specimen it became feasible to determine the molecular mass and mass distribution within individual macromolecules and from these data to calculate the linear density (M/L) and the radii of gyration.2 This parameter (RQ), reflecting the three-dimensional structure of the macromolecular particles in solution, has been applied to monitor the conformational transitions in E. coli 16S and 23S ribosomal RNAs in solutions of various ionic strength.In spite of the differences in mass (550 kD and 1050 kD, respectively), both 16S and 23S RNA appear equally sensitive to changes in buffer conditions. In deionized water or conditions of extremely low ionic strength both appear as filamentous structures (Fig. la and 2a, respectively) possessing a major backbone with protruding branches which are more frequent and more complex in 23S RNA (Fig. 2a).

An Evaluation of a Plasma Fractionation System

1960 ◽  
Vol 4 (01) ◽  
pp. 031-044
Author(s):  
George Y. Shinowara ◽  
E. Mary Ruth
Keyword(s):  
Biological Activity ◽  
Ionic Strength ◽  
Plasma Proteins ◽  
High Concentration ◽  
Significant Evidence ◽  
Native Proteins ◽  
Mobility Data ◽  
Fractionation Procedure ◽  
The Individual ◽  
Low Ionic Strength

SummaryFour primary fractions comprising at least 97 per cent of the plasma proteins have been critically appraised for evidence of denaturation arising from a low temperature—low ionic strength fractionation system. The results in addition to those referable to the recovery of mass and biological activity include the following: The high solubilities of these fractions at pH 7.3 and low ionic strengths; the compatibility of the electrophoretic and ultracentrifugal data of the individual fractions with those of the original plasma; and the recovery of hemoglobin, not hematin, in fraction III obtained from specimens contaminated with this pigment. However, the most significant evidence for minimum alterations of native proteins was that the S20, w and the electrophoretic mobility data on the physically recombined fractions were identical to those found on whole plasma.The fractionation procedure examined here quantitatively isolates fibrinogen, prothrombin and antithrombin in primary fractions. Results have been obtained demonstrating its significance in other biological systems. These include the following: The finding of 5 S20, w classes in the 4 primary fractions; the occurrence of more than 90 per cent of the plasma gamma globulins in fraction III; the 98 per cent pure albumin in fraction IV; and, finally, the high concentration of beta lipoproteins in fraction II.

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