scholarly journals The Isolation and Properties of Some Soluble Proteins From Wool

1964 ◽  
Vol 17 (2) ◽  
pp. 548 ◽  
Author(s):  
JM Gillespie ◽  
PJ Reis ◽  
PG Schinckel
Keyword(s):  
Amino Acids ◽  
Electron Micrographs ◽  
Soluble Proteins ◽  
Sulphur Content ◽  
Rate Of Growth ◽  
Wool Proteins

The proteins in wools of increased sulphur content, grown during abomasal infusions of casein and sulphur-containing amino acids, have been compared with those from control wools from the same sheep. It has been found that casein. methionine, or cysteine administered directly into the abomasum of the sheep, besides increasing the rate of growth of wool, greatly altered the composition of the wool proteins. The proportion of the high-sulphur proteins in wool was increased and within the group of high-sulphur proteins there was increased formation of the components richer in sulphur. No change other than the expected decrease in relative amount can be detected with the low-sulphur proteins. In electron micrographs of the test wool increased amounts of osmiophilic material can be seen in the para segment of the fibre.

scholarly journals The Influence of Sulphur-Containing Amino Acids on the Biosynthesis of High-Sulphur Wool Proteins

1970 ◽  
Vol 23 (1) ◽  
pp. 149 ◽  
Author(s):  
Andrea Broad ◽  
JM Gillespie ◽  
PJ Reis
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Linear Relationship ◽  
Maximum Rate ◽  
Major Part ◽  
Sulphur Content ◽  
Amino Acid Residues ◽  
Deficient Diet ◽  
Methionine Supplementation ◽  
Wool Proteins

The sulphur content of wool can vary within the range of about 2·7-4·2% depending on the diet of the sheep. The lower limit may represent a limiting fundamental structure for wool as it has not been possible to produce wool of sulphur content lower than 2·7% during sulphur-deprivation experiments. There is a highly significant linear relationship between the sulphur content of wool and its content of high-sulphur proteins. The major part of this variation in sulphur content is due to alterations in the extent of biosynthesis of proteins of extremely high sulphur content having about one-third of the amino acid residues presen1, as half cystine. The biosynthesis of these proteins may be under separate metabolic control for they can be produced at maximum rate under conditions where the synthesis of other highsulphur proteins is partly inhibited by a sulphur-deficient diet or by high levels of DL-methionine supplementation

Etude des protéines des blés résistant, Kharkov, et sensible, Selkirk, au cours de l'endurcissement au froid. I. Protéines solubles

1975 ◽  
Vol 53 (21) ◽  
pp. 2411-2416 ◽  
Author(s):  
E. Rochat ◽  
H. P. Therrien
Keyword(s):  
Amino Acids ◽  
Triticum Aestivum ◽  
Triticum Aestivum L ◽  
Soluble Proteins ◽  
Cold Hardening ◽  
Ice Formation

Electrophoregrams of soluble proteins of winter wheats (Triticum aestivum L.) after incorporation of L-[14C] leucine disclose the synthesis of two particular proteins during the cold hardening processes of the hardier variety, Kharkov, compared with a less-hardy variety, Selkirk. The composition in amino acids of the two proteins has been studied and shown to confer them a higher degree of hydrophily making them capable to bind and retain vital water with enough energy to avoid too much dehydration resulting in denaturation during extracellular ice formation.

scholarly journals Biochemical metabolism of two cultivars of cowpea treated with 24-Epibrassinolide and subjected to saline stress

2019 ◽  
Vol 13 ((03) 2019) ◽  
pp. 444-451
Author(s):  
Kerolém Prícila Sousa Cardoso ◽  
Susana Silva Conceição ◽  
Ana Ecídia de Araújo Brito ◽  
Jéssica Taynara da Silva Martins ◽  
Liliane Corrêa Machado ◽  
...  
Keyword(s):  
Amino Acids ◽  
Nitrate Reductase ◽  
Water Content ◽  
Glycine Betaine ◽  
Electrolyte Leakage ◽  
Relative Water Content ◽  
Reductase Activity ◽  
Soluble Proteins ◽  
Saline Stress ◽  
Relative Water

We aimed to evaluate the changes in biochemical metabolism generated by salt stress and to investigate the effect of brassinosteroids in mitigating of this stress on two cultivars of Vigna unguiculata L. We used a completely randomized experimental design in a 2 x 3 x 3 factorial scheme, using two cultivars of cowpea (BRS Guariba and BR3 Tracuateua - moderately tolerant and sensitive to salinity, respectively), three concentrations of brassinosteroids (0, 0.2 and 0.4 μM Br) and three concentrations of NaCl (0 , 50 and 100 mM NaCl), with four replicates. The following evaluations were carried out: relative water content, electrolyte leakage, nitrate levels, nitrate reductase activity, free ammonium, total soluble amino acids, soluble proteins, glycine betaine and proline. The results showed that salinity at 100 mM affected the nitrate reductase enzyme activity, the relative water content, total soluble amino acids and soluble proteins for cultivars BR3 Tracuateua, and BRS Guariba, but the 24-epibrassinolid attenuated the effects of salinity for these variables. The concentration of 0.2 μM of Br increased 55% and 20% in proline and glycine betaine contents, respectively, in both of cultivars. The plants under stress saline and 0.2 mM of 24-epibrassinolid, presented 42% and 58% reductions in electrolyte leakage of BR3 Tracuateua and BRS Guariba cultivars, respectively. The concentrations of ammonium were slightly varied. Therefore, the application of 0.2 μM of 24-epibrassinolid caused a greater acclimatization of the cultivars, being the BR3 Tracuateua (sensitive to salt) cultivar more expressive in most treatments.

A Study of the Ultraviolet Yellowing of Amino Acids, Peptides, and Soluble Proteins

1970 ◽  
Vol 40 (3) ◽  
pp. 285-289 ◽  
Author(s):  
R.S. Asquith ◽  
L. Hirst ◽  
D.E. Rivett
Keyword(s):  
Amino Acids ◽  
Soluble Proteins

Free sugars, amino acids, and soluble proteins in the embryo and female gametophyte of jack pine as related to climate at the seed source

1968 ◽  
Vol 46 (4) ◽  
pp. 417-428 ◽  
Author(s):  
D. J. Durzan ◽  
V. Chalupa
Keyword(s):  
Amino Acids ◽  
Female Gametophyte ◽  
Climatic Factors ◽  
Protein Pattern ◽  
Jack Pine ◽  
Soluble Proteins ◽  
Seed Source ◽  
Chemical Components ◽  
Free Sugars ◽  
Nitrogenous Compounds

Non-stratified and dormant seeds from various geographic sources across the natural range of jack pine (Pinus banksiana Lamb.) were separated into embryo (diploid) and female gametophyte (haploid) and examined for their free sugars, free and bound amino acids, and soluble proteins. Climatic factors from not less than 8 and as many as 15 widely separated seed sources correlated well with most chemical components of the embryo and gametophyte. The composition of the dormant embryo was also highly correlated to levels of sugars and nitrogenous compounds in the female gametophyte. Climate at the seed source clearly affected the degree to which metabolism of carbon and nitrogenous compounds in the seed proceeded before and during incipient germination. Upon germination of seeds from one of the sources, the gametophyte was rapidly consumed, arginine level and protein pattern in the embryo changed, many soluble proteins disappeared and amide content increased greatly.

scholarly journals Omasal Flow of Soluble Proteins, Peptides, and Free Amino Acids in Dairy Cows Fed Diets Supplemented with Proteins of Varying Ruminal Degradabilities

2007 ◽  
Vol 90 (4) ◽  
pp. 1887-1903 ◽  
Author(s):  
S.M. Reynal ◽  
I.R. Ipharraguerre ◽  
M. Liñeiro ◽  
A.F. Brito ◽  
G.A. Broderick ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dairy Cows ◽  
Free Amino Acids ◽  
Free Amino ◽  
Soluble Proteins

scholarly journals PtdIns4P-mediated electrostatic forces influence S-acylation of peripheral proteins at the Golgi complex

2020 ◽  
Vol 40 (1) ◽  
Author(s):  
Sabrina Chumpen Ramirez ◽  
Micaela R. Astrada ◽  
Jose L. Daniotti
Keyword(s):  
Amino Acids ◽  
Golgi Complex ◽  
Electrostatic Interactions ◽  
Transmembrane Protein ◽  
Basic Amino Acid ◽  
Soluble Proteins ◽  
Post Translational Modification ◽  
Hydrophobic Region ◽  
Membrane Interaction ◽  
Basic Amino Acids

Abstract Protein S-acylation is a reversible post-translational modification involving the addition of fatty acids to cysteines and is catalyzed by transmembrane protein acyltransferases (PATs) mainly expressed at the Golgi complex. In case of soluble proteins, S-acylation confers stable membrane attachment. Myristoylation or farnesylation of many soluble proteins constitutes the initial transient membrane adsorption step prior to S-acylation. However, some S-acylated soluble proteins, such as the neuronal growth-associated protein Growth-associated protein-43 (GAP-43), lack the hydrophobic modifications required for this initial membrane interaction. The signals for GAP-43 S-acylation are confined to the first 13 amino acids, including the S-acylatable cysteines 3 and 4 embedded in a hydrophobic region, followed by a cluster of basic amino acids. We found that mutation of critical basic amino acids drastically reduced membrane interaction and hence S-acylation of GAP-43. Interestingly, acute depletion of phosphatidylinositol 4-phosphate (PtdIns4P) at the Golgi complex reduced GAP-43 membrane binding, highlighting a new, pivotal role for this anionic lipid and supporting the idea that basic amino acid residues are involved in the electrostatic interactions between GAP-43 and membranes of the Golgi complex where they are S-acylated.

Small membrane proteins – elucidating the function of the needle in the haystack

2014 ◽  
Vol 395 (12) ◽  
pp. 1365-1377 ◽  
Author(s):  
Grant Kemp ◽  
Florian Cymer
Keyword(s):  
Amino Acids ◽  
Membrane Proteins ◽  
Soluble Proteins ◽  
Structure And Function ◽  
Ribosome Profiling ◽  
Water Soluble ◽  
Eukaryotic Cells ◽  
Large Numbers ◽  
A Cell ◽  
And Function

Abstract Membrane proteins are important mediators between the cell and its environment or between different compartments within a cell. However, much less is known about the structure and function of membrane proteins compared to water-soluble proteins. Moreover, until recently a subset of membrane proteins, those shorter than 100 amino acids, have almost completely evaded detection as a result of technical difficulties. These small membrane proteins (SMPs) have been underrepresented in most genomic and proteomic screens of both pro- and eukaryotic cells and, hence, we know much less about their functions in both. Currently, through a combination of bioinformatics, ribosome profiling, and more sensitive proteomics, large numbers of SMPs are being identified and characterized. Herein we describe recent advances in identifying SMPs from genomic and proteomic datasets and describe examples where SMPs have been successfully characterized biochemically. Finally we give an overview of identified functions of SMPs and speculate on the possible roles SMPs play in the cell.

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