A Water-soluble Arabinogalactan-Peptide From Wheat Endosperm

1974 ◽  
Vol 27 (2) ◽  
pp. 117 ◽  
Author(s):  
GB Fincher ◽  
BA Stone
Keyword(s):  
Protein A ◽  
Water Extract ◽  
Water Soluble ◽  
Low Molecular Weight ◽  
Density Gradient Ultracentrifugation ◽  
Ethanol Treatment ◽  
Material Density ◽  
Wheat Endosperm ◽  
Caesium Chloride ◽  
Polymeric Fraction

The water-soluble polymeric components of wheat endosperm have been extracted by two different procedures and their chemical composition studied in detail. Water extracts of wheat flour that had first been treated with hot 80% ethanol contained only 2% protein, but if the ethanol treatment was omitted up to 20% of the extracted polymeric fraction was low-molecular-weight non-dialysable protein material. Density-gradient ultracentrifugation in caesium chloride solutions indicated that most of this protein was free, whereas the 2% protein in the water extract of ethanol-treated flottr was firmly bound to a polysaccharide. This bound protein (a peptide) was characterized by high levels of hydroxyproline (16-20% of the amino acids present).

ANALISA KANDUNGAN BETA-GLUKAN LARUT AIR DAN LARUT ALKALI DARI TUBUH BUAH JAMUR TIRAM (Pleurotus ostreatus) DAN SHIITAKE (Lentinus edodes)

2013 ◽  
Vol 13 (3) ◽  
Author(s):  
Netty Widyastuti ◽  
Teguh Baruji ◽  
Henky Isnawan ◽  
Priyo Wahyudi ◽  
Donowati Donowati
Keyword(s):  
Molecular Structure ◽  
Molecular Weight ◽  
Immune System ◽  
Pleurotus Ostreatus ◽  
Water Soluble ◽  
Low Molecular Weight ◽  
Lentinus Edodes ◽  
Beta Glucan ◽  
Oyster Mushrooms ◽  
The Difference

Beta glucan is a polysaccharide compound, generally not soluble inwater and resistant to acid. Beta glucan is used as an immunomodulator (enhancing the immune system) in mammals is usually a beta-glucan soluble in water, easily absorbed and has a low molecular weight. Several example of beta-glucan such as cellulose (β-1 ,4-glucan), lentinan (β-1 0.6-glucan) and (β-1 ,3-glucan), pleuran (β-1, 6 and β-1 ,3-glucan) are isolated from species of fungi Basidiomycota include mushrooms (Pleurotus ostreatus) and shiitake (Lentinus edodes).The purpose of thisresearch activity is to obtain beta-glucan compound that can be dissolved in water and in alkali derived from fungi Basidiomycota, i.e, Oyster mushrooms (Pleurotus ostreatus) and shiitake (Lentinus edodes). The result of beta-glucan compared to characterize the resulting beta glucan that is molecular structure . The difference of beta glucan extraction is based on the differences in solubility of beta-glucan. Beta glucan could be water soluble and insoluble water.

scholarly journals Isolation of human synovial-fluid hyaluronate by density-gradient ultracentrifugation and evaluation of its protein content

1972 ◽  
Vol 126 (5) ◽  
pp. 1073-1080 ◽  
Author(s):  
Irwin Scher ◽  
David Hamerman
Keyword(s):  
Synovial Fluid ◽  
Density Gradient ◽  
Density Gradient Ultracentrifugation ◽  
Proteolytic Digestion ◽  
Peptide Fragments ◽  
Guanidinium Chloride ◽  
Caesium Chloride ◽  
Normal Human ◽  
Protein Moiety ◽  
Human Synovial Fluid

1. A compound of hyaluronate and protein, called hyaluronate–protein was isolated from pooled human synovial fluids by caesium chloride density-gradient ultracentrifugation. 2. The isolated hyaluronate–protein was labelled with [125I]iodide and the following studies were done. (a) Ultracentrifugation in caesium chloride showed that the protein moiety (125I counts) and hyaluronate (hexuronate) sedimented together in the middle of the gradient. (b) The labelled hyaluronate–protein was treated with trypsin, and ultracentrifugation showed that peptide fragments (125I counts) were dispersed throughout the gradient, indicating proteolytic digestion. Hyaluronate sedimented in the middle of the gradient. (c) The labelled hyaluronate–protein was digested with streptococcal hyaluronidase, and ultracentrifugation showed that hyaluronate fragments were dispersed throughout the gradient, indicating digestion of the polysaccharide. The protein moiety, without attached hyaluronate, now sedimented at the top of the gradient. (d) Ultracentrifugation of labelled hyaluronate–protein in 4m-guanidinium chloride showed that protein and hyaluronate sedimented together. 3. These studies confirm that hyaluronate is combined with a small quantity of protein in normal human synovial fluid. A mild method for the rapid isolation of hyaluronate–protein in good yield is described.

scholarly journals Water-soluble low-molecular-weight cellulose chains radially oriented on gold nanoparticles

Cellulose ◽  
2011 ◽  
Vol 18 (4) ◽  
pp. 929-936 ◽  
Author(s):  
Yukiko Enomoto-Rogers ◽  
Hiroshi Kamitakahara ◽  
Arata Yoshinaga ◽  
Toshiyuki Takano
Keyword(s):  
Molecular Weight ◽  
Gold Nanoparticles ◽  
Water Soluble ◽  
Low Molecular Weight

scholarly journals Proteolytic and peroxidatic reactions of commercial horseradish peroxidase with myelin basic protein

1978 ◽  
Vol 169 (3) ◽  
pp. 567-575 ◽  
Author(s):  
Wendy Cammer ◽  
Lesley Z. Bieler ◽  
William T. Norton
Keyword(s):  
Horseradish Peroxidase ◽  
Myelin Basic Protein ◽  
Basic Protein ◽  
Protein A ◽  
Low Molecular Weight ◽  
Basic Proteins ◽  
Molecular Weights ◽  
Low Concentrations ◽  
High Concentrations ◽  
A Minor

Degradation of myelin basic protein during incubations with high concentrations of horseradish peroxidase has been demonstrated [Johnson & Cammer (1977) J. Histochem. Cytochem.25, 329–336]. Possible mechanisms for the interaction of the basic protein with peroxidase were investigated in the present study. Because the peroxidase samples previously observed to degrade basic protein were mixtures of isoenzymes, commercial preparations of the separated isoenzymes were tested, and all three degraded basic protein, but to various extents. Three other basic proteins, P2 protein from peripheral nerve myelin, lysozyme and cytochrome c, were not degraded by horseradish peroxidase under the same conditions. Inhibitor studies suggested a minor peroxidatic component in the reaction. Therefore the peroxidatic reaction with basic protein was studied by using low concentrations of peroxidase along with H2O2. Horseradish peroxidase plus H2O2 caused the destruction of basic protein, a reaction inhibited by cyanide, azide, ferrocyanide, tyrosine, di-iodotyrosine and catalase. Lactoperoxidase plus H2O2 and myoglobin plus H2O2 were also effective in destroying the myelin basic protein. Low concentrations of horseradish peroxidase plus H2O2 were not active against other basic proteins, but did destroy casein and fibrinogen. Although high concentrations of peroxidase alone degraded basic protein to low-molecular-weight products, suggesting the operation of a proteolytic enzyme contaminant in the absence of H2O2, incubations with catalytic concentrations of peroxidase in the presence of H2O2 converted basic protein into products with high molecular weights. Our data suggest a mechanism for the latter, peroxidatic, reaction where polymers would form by linking the tyrosine side chains in basic-protein molecules. These data show that the myelin basic protein is unusually susceptible to peroxidatic reactions.

Disparate effects of two phosphatidylcholine binding proteins, C-reactive protein and surfactant protein A, on pulmonary surfactant structure and function

2004 ◽  
Vol 287 (6) ◽  
pp. L1145-L1153 ◽  
Author(s):  
Kaushik Nag ◽  
Karina Rodriguez-Capote ◽  
Amiya Kumar Panda ◽  
Laura Frederick ◽  
Stephen A. Hearn ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Amorphous Material ◽  
Protein A ◽  
Surfactant Protein ◽  
Water Soluble ◽  
Surfactant Protein A ◽  
Surface Films ◽  
Inhibitory Effects ◽  
C Reactive Protein ◽  
Reactive Protein

C-reactive protein (CRP) and surfactant protein A (SP-A) are phosphatidylcholine (PC) binding proteins that function in the innate host defense system. We examined the effects of CRP and SP-A on the surface activity of bovine lipid extract surfactant (BLES), a clinically applied modified natural surfactant. CRP inhibited BLES adsorption to form a surface-active film and the film's ability to lower surface tension (γ) to low values near 0 mN/m during surface area reduction. The inhibitory effects of CRP were reversed by phosphorylcholine, a water-soluble CRP ligand. SP-A enhanced BLES adsorption and its ability to lower γ to low values. Small amounts of SP-A blocked the inhibitory effects of CRP. Electron microscopy showed CRP has little effect on the lipid structure of BLES. SP-A altered BLES multilamellar vesicular structure by generating large, loose bilayer structures that were separated by a fuzzy amorphous material, likely SP-A. These studies indicate that although SP-A and CRP both bind PC, there is a difference in the manner in which they interact with surface films.

Water-soluble low-molecular-weight organic acids in automorphic loamy soils of the tundra and taiga zones

2013 ◽  
Vol 46 (6) ◽  
pp. 654-659 ◽  
Author(s):  
E. V. Shamrikova ◽  
I. V. Gruzdev ◽  
V. V. Punegov ◽  
F. M. Khabibullina ◽  
O. S. Kubik
Keyword(s):  
Molecular Weight ◽  
Organic Acids ◽  
Water Soluble ◽  
Low Molecular Weight
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