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.

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.

Phosphorylation Of Platelet Actin-Binding Protein During Platelet Activation

1981 ◽  
Author(s):  
Roger C Carroll ◽  
Jonathan M Gerrard
Keyword(s):  
Molecular Weight ◽  
Platelet Activation ◽  
Time Course ◽  
Binding Protein ◽  
Sodium Dodecyl ◽  
Apparent Molecular Weight ◽  
Actin Binding ◽  
Actin Binding Protein ◽  
Platelet Protein ◽  
External Calcium

We have followed the 32P-labelling of actin-binding protein as a function of platelet activation. Utilizing polyacrylamide sodium dodecyl sulfate gel electrophoresis to resolve total platelet protein samples we found 2 to 3 fold labelling increases in actin-binding protein 30 to 60 seconds after thrombin stimulation. Somewhat larger increases were observed for 40,000 and 20,000 apparent molecular weight peptides. The actin-binding protein was identified on the gels by coelectrophoresis of purified actin-binding protein as well as cytoskeletal cores prepared by detergent extraction of activated 32p-iabelled platelets. In addition, these cytoskeletal cores indicated that the 32P-labelled actin-binding protein was closely associated with the activated platelet's cytoskeleton. Following the 32P-labelling of actin-binding protein over an 8 minute time course revealed that in aggregating platelet samples rapid desphosphorylation to almost initial levels occurred between 3 and 5 minutes. A similar curve was obtained for the 20,000 apparent molecular weight peptide. This rapid dephosphorylation was shown to be dependent on platelet aggregation in the absence of external calcium or in thrombastenic platelets lacking the aggregation response to activation. These results suggest that phosphorylation of actin-binding protein initiates its association with the platelet cytoskeleton during activation.

Structure and characterization of the gene encoding the ferredoxin-NADP reductase-binding protein from Zea mays L.

Gene ◽  
1994 ◽  
Vol 147 (2) ◽  
pp. 205-208 ◽  
Author(s):  
Silvina Pessino ◽  
Carme Caelles ◽  
Pere Puigdomènech ◽  
Rubén H. Vallejos
Keyword(s):  
Zea Mays ◽  
Zea Mays L ◽  
Binding Protein ◽  
Gene Encoding

scholarly journals Studies on the appearance of a hepatic copper-binding protein in normal and zinc-deficient rats

1976 ◽  
Vol 36 (1) ◽  
pp. 101-112 ◽  
Author(s):  
I. Bremner ◽  
N. T. Davies
Keyword(s):  
Molecular Weight ◽  
Metal Binding ◽  
Binding Protein ◽  
Gel Filtration ◽  
Apparent Molecular Weight ◽  
Low Molecular Weight ◽  
Copper Binding ◽  
Hepatic Copper ◽  
Copper Binding Protein ◽  
Molecular Weight Form

1. A study has been made by gel-filtration techniques of the soluble copper- and zinc-binding proteins in rat liver after both intraperitoneal injection of Cu and dietary Cu supplementation.2. Liver Cu and Zn concentrations increased after injection of Cu, both metals accumulating in the cytosol, mainly in a fraction with an apparent molecular weight of (about 12 000)3. When Zn-deficient rats were injected with Cu, there was little change in liver Zn concentration and the occurrence of Cu in the low-molecular-weight form (about 12 000) was more transient. At most periods after injection, Cu accumulated mainly in a fraction with a molecular weight greater than 65 000.4. When the rats were Cu-loaded by dietary supplementation, virtually no Cu or Zn was found in the low-molecular-weight form in Zn-deficient rats, although they were found in the Zn-supplemented animals.5. The results suggest that Zn is essential for the accumulation of Cu in this form, but not for Cu to stimulate production of the metal-binding protein by a process requiring active protein synthesis.

scholarly journals Study on the interaction of Zea mays L. centrin and melittin

RSC Advances ◽  
2021 ◽  
Vol 11 (57) ◽  
pp. 36098-36104
Author(s):  
Zhijun Wang ◽  
Yanlong Feng ◽  
Tiantian Song ◽  
Jie Su ◽  
Mengjie Fu ◽  
...  
Keyword(s):  
Zea Mays ◽  
Calcium Binding ◽  
Zea Mays L ◽  
Binding Protein ◽  
Calcium Binding Protein

Zea mays L. centrin (Zmcen) is a 20 kDa calcium binding protein also known as caltractin.

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