Metal binding properties of high molecular weight soluble exudates from maize (Zea mays L.) roots

1987 ◽  
Vol 3 (3) ◽  
pp. 165-169 ◽  
Author(s):  
M. Mench ◽  
J.L. Morel ◽  
A. Guckert
Keyword(s):  
Molecular Weight ◽  
Zea Mays ◽  
High Molecular Weight ◽  
Metal Binding ◽  
Zea Mays L ◽  
Binding Properties

VARIATION IN THE DIFFERENTIAL LEAF ABSORPTION OF A HIGH-MOLECULAR-WEIGHT PHOSPHATE BY PLANTS OF DIFFERING CYTOPLASMS OF THREE CORN (ZEA MAYS) INBREDS

1975 ◽  
Vol 17 (2) ◽  
pp. 211-216 ◽  
Author(s):  
Dirk Barèl ◽  
Peter A. Peterson
Keyword(s):  
Molecular Weight ◽  
Zea Mays ◽  
Membrane Permeability ◽  
High Molecular Weight ◽  
Zea Mays L ◽  
Male Sterile ◽  
Cytoplasmic Male Sterile ◽  
Rate Of Absorption

The absorption of foliarly applied tripolyphosphate is significantly greater in two different cytoplasmically male-sterile lines (Tcms and Ccms) of Zea mays L. than in isolines having normal (N) cytoplasm. A third cytoplasmic male-sterile (Scms) does not differ from the normal isoline in its absorption of foliarly applied tripolyphosphate. In none of the three comparisons of each of the cytoplasmic male-sterile lines and its normal isoline is there a difference in orthophosphate absorption, nor do any of the lines show a difference in the translocation of either source of phosphorus (P) inside the plant 10 days after application. The differential uptake of the large molecular P compound is not a property of all cytoplasmic male steriles, indicating that all cytoplasmic male steriles, do not have similar membrane permeability properties. Differences were found in the rate of absorption among lines for foliarly applied phosphates.

scholarly journals Bioaccumulation of silver and the isolation of metal-binding protein from P.diminuta

2001 ◽  
Vol 44 (3) ◽  
pp. 223-225 ◽  
Author(s):  
Zaharah Ibrahim ◽  
Wan Azlina Ahmad ◽  
Abu Bakar Baba
Keyword(s):  
Molecular Weight ◽  
Metal Binding ◽  
Metal Uptake ◽  
Silver Ions ◽  
Low Molecular Weight ◽  
Early Exponential Phase ◽  
Binding Properties ◽  
Bacterial Cultures ◽  
Sds Page ◽  
Pseudomonas Diminuta

A silver uptake study by Pseudomonas diminuta was carried out by growing the bacteria in a chloride-free medium (CFM) containing silver ions (50 muM) in a batch culture. From the results, it was found that higher amounts of silver were accumulated inside the cell during early exponential phase compared to the amount bound at the cell surface. This suggested a possible mechanism for metal uptake during bacterial growth. In view of this, attempts were made to isolate proteins which might be associated with silver-binding properties from cultures of P.diminuta grown in the presence and absence of silver. The proteins were first extracted from the bacterial cultures by precipitation with ammonium sulfate followed by purification using isoelectric focussing and SDS-PAGE. Results of the experiment showed the presence of low molecular weight and high molecular weight proteins containing silver with pI values ranging from 2.0 to 9.0 for bacteria grown in the presence of silver.

scholarly journals Single-chain polybutadiene organometallic nanoparticles: an experimental and theoretical study

2016 ◽  
Vol 7 (3) ◽  
pp. 1773-1778 ◽  
Author(s):  
Inbal Berkovich ◽  
Sudheendran Mavila ◽  
Olga Iliashevsky ◽  
Sebastian Kozuch ◽  
N. Gabriel Lemcoff
Keyword(s):  
Molecular Weight ◽  
Double Bond ◽  
High Molecular Weight ◽  
Metal Binding ◽  
Theoretical Study ◽  
Binding Kinetics ◽  
Rhodium Complexes ◽  
Single Chain ◽  
Double Bond Content

High molecular weight polybutadienes and rhodium complexes were used to produce single chain organometallic nanoparticles. A relationship was found between the cis double bond content of the polymer and metal binding kinetics.

Cadmium-binding protein in roots of maize

1984 ◽  
Vol 62 (8) ◽  
pp. 1645-1650 ◽  
Author(s):  
Wilfried E. Rauser ◽  
John Glover
Keyword(s):  
Molecular Weight ◽  
Zea Mays ◽  
Anion Exchanger ◽  
Zea Mays L ◽  
Binding Protein ◽  
Apparent Molecular Weight ◽  
Protein Preparation ◽  
Spectroscopic Measurements ◽  
Cysteine Content ◽  
L Proteins

A partially purified cadmium (Cd) binding protein was isolated from roots of maize (Zea mays L.). Proteins were first separated on the anion exchanger QAE-Sephadex A-25. The major Cd fraction, comprising as much as 85% of the buffer-soluble Cd, was then chromatographed on Sephadex G-75 in 1 M KCl buffer. The resulting partially purified protein preparation was dark brown, had an apparent molecular weight of 3100, and bound 2 g atoms Cd/mol. The cysteine content was 40%; the Cd:cysteine ratio was 1:6. The Cd–thiolate chromophore was evident from spectroscopic measurements. The roots produced the metallothioneinlike protein after they were exposed to 3 μM Cd for 4 days.

Sign in / Sign up

Export Citation Format

Share Document