The Carbohydrate Moiety of Mung Bean Vicilin

1976 ◽  
Vol 3 (6) ◽  
pp. 763 ◽  
Author(s):  
MC Ericson ◽  
MJ Chrispeels
Keyword(s):  
Mung Bean ◽  
Deae Cellulose ◽  
Indirect Evidence ◽  
Carbohydrate Moiety ◽  
Side Chain ◽  
Phaseolus Aureus ◽  
Molecular Weights ◽  
Molar Ratios ◽  
Peptide Moiety ◽  
Carbohydrate Unit

Mung bean (Phaseolus aureus Roxb.) vicilin, purified by DEAE-cellulose chromatography, is a glycoprotein (0.2% glucosamine and 1% mannose) which contains four different polypeptides with molecular weights of 63 500, 50000, 29 500 and 24 000 in the molar ratios 1 : 5 : 1 : 1. Two of these polypeptides (50 000 and 29 500) stain positively for carbohydrate. When vicilin is digested with pronase, the carbohydrate can be recovered as a glycopeptide containing mannose and glucosamine in the carbohydrate moiety and alanine, threonine and aspartic acid (or asparagine) in the peptide moiety. The total amount of carbohydrate (1.2 %) and the size of the carbohydrate unit (12 residues) suggest that each vicilin molecule contains only one carbohydrate side chain. Data indicate that this chain is attached via a glucosamine-asparagine link. The results raise the possibility that the presence of the two small polypeptides in vicilin preparations is the result of the breakdown of the major larger one. Indirect evidence suggests that vicilin may be a tetramer of four subunits, each with a molecular weight of 50 000, and that only one subunit has a carbohydrate side chain.

scholarly journals Purification and subunit analysis of wheat-germ ribonucleic acid polymerase II

1974 ◽  
Vol 139 (3) ◽  
pp. 771-777 ◽  
Author(s):  
Jerome J. Jendrisak ◽  
Wayne M. Becker
Keyword(s):  
Enzyme Activity ◽  
Rna Polymerase ◽  
Wheat Germ ◽  
Sucrose Gradient ◽  
Gradient Centrifugation ◽  
Deae Cellulose ◽  
Protamine Sulphate ◽  
Molecular Weights ◽  
Molar Ratios ◽  
High Salt Buffer

A procedure is described for the purification of the α-amanitin-sensitive DNA-dependent RNA polymerase [EC 2.7.7.6] from wheat germ. Solubilization of the enzyme activity was achieved by sonication of a crude extract in a high-salt buffer. Purification involved precipitation with protamine sulphate and (NH4)2SO4, chromatography on DEAE-cellulose and phosphocellulose, and sucrose gradient centrifugation. Under denaturing conditions the enzyme dissociated into five polypeptides with molecular weights and molar ratios of 220000 (0.9), 170000 (0.1), 140000 (1.0), 45000 (0.2), and 40000 (0.4). Approx. 1mg of purified RNA polymerase was obtained as a routine from 100g of starting material.

TRANSAMINATION IN PLANTS: THE SPECIFICITY OF AN AMINOTRANSFERASE FROM MUNG BEAN

1965 ◽  
Vol 43 (6) ◽  
pp. 723-730 ◽  
Author(s):  
Oluf L. Gamborg
Keyword(s):  
Amino Acids ◽  
Ammonium Sulfate ◽  
Mung Bean ◽  
Deae Cellulose ◽  
Phaseolus Aureus ◽  
Ammonium Sulfate Precipitation ◽  
Competitive Inhibitors

A study has been made of the specificity of an aminotransferase from mung bean (Phaseolus aureus Roxb.). The enzyme was purified 40- to 60-fold by using Sephadex G-50, ammonium sulfate precipitation, DEAE-cellulose, and hydroxylapatite. In the presence of pyruvate the enzyme transaminated a number of cyclic and aliphatic amino acids. Some of the better substrates were lysine, arginine, ornithine, glutamine, methionine, leucine, 4-fiuorophenyl-alanine, phenylalanine, tyrosine, tryptophan, 3,4-dihydroxyphenylalanine, and γ-phenylbutyrine. Threonine, serine, and glycine were not transaminated. Lysine, methionine, and glutamate were competitive inhibitors of the transamination of phenylalanine.

scholarly journals SOME PROTEINS FROM THE MUNG BEAN, PHASEOLUS AUREUS ROXBURGH

1920 ◽  
Vol 44 (2) ◽  
pp. 303-317
Author(s):  
Carl O. Johns ◽  
Henry C. Waterman
Keyword(s):  
Mung Bean ◽  
Phaseolus Aureus

scholarly journals INVESTIGATIONS ON THE MUNG BEAN (PHASEOLUS AUREUS ROXBURGH)

1948 ◽  
Vol 175 (1) ◽  
pp. 377-383
Author(s):  
W. Edward Belton ◽  
Cecile A. Hoover
Keyword(s):  
Mung Bean ◽  
Phaseolus Aureus

Comparison of the conformation and stability of the native dimeric, monomelic, tetrameric and the desensitized forms of the nucleotide pyrophosphatase from mung bean (Phaseolus aureus) seedlings

1980 ◽  
Vol 2 (3) ◽  
pp. 211-225 ◽  
Author(s):  
A. R. Venugopala Reddy ◽  
C. V. Balakrishnan ◽  
J. Sobhanaditya ◽  
S. D. Ravindranath ◽  
V. S. Ananthanarayanan ◽  
...  
Keyword(s):  
Mung Bean ◽  
Phaseolus Aureus ◽  
Nucleotide Pyrophosphatase

scholarly journals The macromolecular properties of blood-group-specific glycoproteins. Characterization of a series of fractions obtained by density-gradient ultracentrifugation

1974 ◽  
Vol 143 (3) ◽  
pp. 669-679 ◽  
Author(s):  
K. Ramakrishnan Bhaskar ◽  
J. Michael Creeth
Keyword(s):  
Density Gradient ◽  
Blood Group ◽  
Buoyant Density ◽  
Physicochemical Characterization ◽  
Cyst Fluid ◽  
Equilibrium Density ◽  
Density Gradient Ultracentrifugation ◽  
Molecular Weights ◽  
Molar Ratios ◽  
Blood Group Substances

1. Equilibrium density-gradient ultracentrifugation in caesium salts was used in two stages in the isolation and subfractionation of the glycoprotein component from a human ovarian-cyst fluid. The eight main subfractions thus obtained were the subject of detailed physicochemical characterization. 2. The fractions were unimodal in buoyant-density distribution, but had discrete ρ0 values ranging from 1.31 to 1.35. 3. Weight-average molecular weights and sedimentation coefficients decreased regularly with decreasing density of the fraction, whereas the partial specific volumes and selective solvation parameters increased. The latter behaviour correlates well with the increasing peptide content of the lighter fractions. 4. The fractions exhibited a range of analytical composition, although all were within the limits previously observed for blood-group substances of Lea specificity. All fractions had approximately equal Lea activity. The peptide content varied systematically from 7% for the densest fraction to 15% for the lightest, but the relative distributions of the amino acids remained essentially constant throughout the series. In particular, serine plus threonine plus proline made up about 50% of the peptide content of all the fractions. Fucose, galactose and N-acetylglucosamine contents decreased with increasing peptide content of the fractions, but N-acetylgalactosamine and sialic acid exhibited the opposite trend. Molar ratios of N-acetylgalactosamine to the sum of serine and threonine remained essentially constant at 0.8–0.9, implying a high degree of glycosylation of all the molecules, but the ratio of N-acetylglucosamine to N-acetylgalactosamine decreased steadily with increasing peptide content, suggesting the presence of oligosaccharide side chains of various lengths. The results are discussed in terms of the accepted structure of glycoprotein molecules. 5. Experiments on the glycoproteins extracted with phenol from the same cyst fluid have confirmed that equilibrium centrifugation in caesium salts does not remove any non-covalently bound protein nor cause any changes in the tertiary structures of these glycoprotein molecules.

scholarly journals α-Crystallin. The isolation and characterization of distinct macromolecular fractions

1971 ◽  
Vol 124 (2) ◽  
pp. 337-343 ◽  
Author(s):  
Abraham Spector ◽  
Lu-Ku Li ◽  
Robert C. Augusteyn ◽  
Arthur Schneider ◽  
Thomas Freund
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Chemical Difference ◽  
Molecular Weights ◽  
Isolation And Characterization ◽  
Different Populations ◽  
Molecular Weight Fractions

α-Crystallin was isolated from calf lens periphery by chromatography on DEAE-cellulose and gel filtration. Three distinct populations of macromolecules have been isolated with molecular weights in the ranges approx. 6×105−9×105, 0.9×106−4×106and greater than 10×106. The concentration of macromolecules at the molecular-weight limits of a population are very low. The members of the different populations do not appear to be in equilibrium with each other. Further, in those molecular-weight fractions investigated, no equilibrium between members of the same population was observed. The population of lowest molecular weight comprises 65–75% of the total material. The amino acid and subunit composition of the different-sized fractions appear very similar, if not identical. The only chemical difference observed between the fractions is the presence of significant amounts of sugar in the higher-molecular-weight fractions. Subunit molecular weights of approx. 19.5×103and 22.5×103were observed for all α-crystallin fractions.

Polymerization of n-butyl methylacrylate using bis(β- ketoamino)nickel(II)/MAO catalytic systems

e-Polymers ◽  
2008 ◽  
Vol 8 (1) ◽  
Author(s):  
Xiaohui He ◽  
Yiwang Chen ◽  
Yongming Liu ◽  
Muqing Chen ◽  
Shuxian Yu ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Monomer Concentration ◽  
Polymerization Temperature ◽  
Moderate Activity ◽  
Polymerization Time ◽  
Catalytic Systems ◽  
Molecular Weights ◽  
Molar Ratios ◽  
Broad Molecular Weight Distribution ◽  
C Nmr

AbstractThe polymerizations of n-butyl methylacrylate (nBMA) were carried out using bis(β-ketoamino)nickel(II) complexes (Ni[CH3C(O)CHC(NR)CH3]2: R = phenyl, 1; R = naphthyl, 2) in combination with methylaluminoxane (MAO) in toluene. The effect of parameters such as polymerization temperature, Al/Ni molar ratios, polymerization time, and monomer concentration, on catalytic polymerization activity and polymer molecular weights, were examined in detail. Both of the nickel(II) catalytic systems exhibited moderate activity, and produced P(nBMA) with high molecular weight and relatively broad molecular weight distribution (Mw/Mn=2.0~3.0. The obtained polymer has been characterized by means of FTIR, 1H NMR, 13C NMR, DSC, and WAXD technique and was confirmed to be syndio-rich stereospecific P(nBMA).

Click Synthesis of Shape-Persistent Azodendrimers and their Orthogonal Self-Assembly to Nanofibres

2018 ◽  
Vol 71 (6) ◽  
pp. 463 ◽  
Author(s):  
Tamer El Malah ◽  
Hany F. Nour
Keyword(s):  
Electron Microscopy ◽  
Mass Spectrometry ◽  
Self Assembly ◽  
Molecular Structures ◽  
Side Chain ◽  
Spectroscopic Techniques ◽  
Molecular Weights ◽  
Transmission Electron ◽  
Click Synthesis ◽  
Scanning Electron

The copper(i)-catalyzed azide–alkyne cycloaddition (CuAAC) reaction has been efficiently utilized to synthesize a series of dendrons with amino functionalities. The aminodendrons successfully underwent azodimerization to furnish a series of pyridyl- and phenyl-based azodendrimers with peripheral alkyl or ether side chain substituents. The molecular structures of the azodendrimers were fully assigned using different spectroscopic techniques, such as 1H NMR and 13C NMR, and the molecular weights were determined using MALDI-TOF mass spectrometry. The molecular self-assembly of the azodendrimers was investigated by scanning electron microscopy and transmission electron microscopy, which revealed the formation of highly ordered and uniform self-assembled nanofibres.

Sign in / Sign up

Export Citation Format

Share Document