Wheat glutenin: effect of dissociating agents on molecular weight and composition as determined by gel filtration chromatography

1980 ◽  
Vol 28 (2) ◽  
pp. 433-438 ◽  
Author(s):  
Floyd R. Huebner ◽  
Joseph S. Wall
2003 ◽  
Vol 58 (11-12) ◽  
pp. 891-894 ◽  
Author(s):  
Teruhiko Nitoda ◽  
Hirokazu Usuki ◽  
Hiroshi Kanzaki

Abstract A water-soluble polysaccharide was isolated from the culture filtrate of a fungal strain, Sphaeropsis sp. TNPT116-Cz, as a novel insect chitinase inhibitor. It was purified to chromatographic homogeneity by ethanol precipitation, anion-exchange and gel filtration chromatography. Its molecular weight was estimated to be 16 kDa by gel filtration HPLC. Monosaccharide analysis showed that it contained glucose, galactose, N-acetylglucosamine and a deoxysugar. This polysaccharide showed potent and specific inhibitory activity against Spodoptera litura chitinase with an IC50 value of 28 nᴍ.


1994 ◽  
Vol 40 (3) ◽  
pp. 224-227 ◽  
Author(s):  
E. O. Kalcheva ◽  
M. M. Faiziev ◽  
V. O. Shanskaya ◽  
S. S. Maluta

Streptococcus bovis has been found to contain two distinct aspartokinases that can be separated by gel filtration chromatography. One of these isozymes elutes on Sephadex G-200 gel filtration at a molecular weight greater than 250 000. The molecular weight of the other isozyme is approximately 125 000. The earlier peak of aspartokinase activity is slightly inhibited by meso-diaminopimelate, while the second peak is sensitive to inhibition by lysine. The latter aspartokinase is not formed when the organism is grown in a medium containing more than 1 mM lysine. The level of lysine-sensitive aspartokinase is decreased during the growth cycle, whereas diaminopimelate-sensitive activity is little affected by the growth conditions. The regulatory properties of the two aspartokinases suggest that they may play different physiological roles.Key words: aspartokinase activity, isozymes, repression, inhibition.


1975 ◽  
Vol 53 (5) ◽  
pp. 574-582
Author(s):  
Francesco Moranelli ◽  
P. E. Penner

A ribonuclease-sensitive DNA polymerase, which uses an endogenous template, is detectable in the 39 000 g supernatant of a rat thymus homogenate, and appears as a single peak of activity in the void volume after Sephadex G 150 or G 200 gel filtration chromatography. Native and "activated" DNA-dependent DNA polymerase activities coincide with the endogenous-templated polymerase activity. Treatment of the thymus extract with ribonuclease(s) prior to gel filtration chromatography yields two other peaks of activity in addition to the void volume peak. The appearance of the two lower molecular weight peaks of activity is accompanied by a concomitant decrease in the endogenous-templated activity. The effect of ribonuclease is specific and cannot be reproduced by a similar deoxyribonuclease treatment.


2012 ◽  
Vol 6 (2) ◽  
pp. 15-22
Author(s):  
Mouruj A. Alaubydi ◽  
Susan Ahmad ◽  
Muayad Sabri

ipopolysaccharide was extracted from local isolate Sallmonella typhi (previously isolated and characterized) by hot EDTA method, and the extract was partially purified by gel filtration chromatography on sepharose Cl-6B gel. The results showed that the percentage of the carbohydrates amount in the partially purified LPS extract was 43.7%, while the percentage of binding proteins in the same extract was 0.7% with no nucleic acids was found. The molecular weight for the LPS was measured by the gel filtration chromatography method using Sepharose Cl-6B gel and was equivalent to 263000 Dalton. The LD¬50 of LPS was determined by injection of chicken embryos type Ice Brown in the charioallantoic membrane, and was 14.66 µg/Kg. In order to obtain anti S. typhi IgY antibodies, chickens were immunized with the partially purified S. typhi subcutaneously. The IgY antibodies were extracted from eggs yolk by water dilution method and the extract was partially purified by ammonium sulphate precipitation at ratio 60% saturation, and gel filtration chromatography on sepharose Cl-6B gel. The results showed that the protein amount was equivalent to 23.5 mg/ml; specific activity was 0.268, and an overall yield of 70%. The molecular weight for the IgY antibodies was measured by the gel filtration chromatography method using Sepharose Cl-6B gel and was found to be 178000 dalton. The concentration of anti S.typhi LPS IgY antibodies in chicken eggs were investigated by ELISA and was found to be 6.3 mg/ml, and there is a significant differences (P<0.01).


2011 ◽  
Vol 183-185 ◽  
pp. 1132-1136
Author(s):  
Hui Wang ◽  
Han Sheng Gong ◽  
Xiang Chen Meng ◽  
Li Li Man

A bacteriocin produced by Lactobacillus brevis KLDS1.0373 which was isolated from “Jiaoke”, a traditional, naturally fermented cream from Inner Mongolia in China was reported in this article. The bacteriocin was partially purified by ammonium sulfate precipitation followed by sequential gel filtration chromatography, and the apparent molecular weight of the partially purified bacteriocin was estimated at approximately 3.8 kDa.


1981 ◽  
Vol 199 (3) ◽  
pp. 807-811 ◽  
Author(s):  
G Murphy ◽  
T E Cawston ◽  
W A Galloway ◽  
M J Barnes ◽  
R A D Bunning ◽  
...  

Gel-filtration chromatography of culture medium from rabbit bone explants separates three latent metalloproteinases with activities against collagen, proteoglycan and gelatin respectively. The fractions degrading proteoglycan also degrade laminin, fibronectin and the polymeric products of pepsin-solubilized type IV collagen and can also solubilize insoluble type IV collagen. The fractions degrading gelatin are capable of degrading solubilized type V and 1 alpha,2 alpha,3 alpha (cartilage) collagens, as well as the lower-molecular-weight products of pepsin-solubilized type IV collagen. All activities can be inhibited by 1,10-phenanthroline and occur in either partially or totally latent forms that can be activated by 4-aminophenylmercuric acetate.


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