Structural Studies on Antigen E of Ragweed Pollen

1973 ◽  
Vol 51 (9) ◽  
pp. 1275-1280 ◽  
Author(s):  
B. W. Griffiths
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Reducing Agent ◽  
Ragweed Pollen ◽  
Gel Chromatography ◽  
Structural Studies ◽  
Molecular Weights ◽  
Polypeptide Chains

The analysis of antigen E of ragweed pollen by polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS) resulted in the demonstration of two subunits of molecular weights of about 20 000 and 14 500. These results confirm earlier studies on antigen E by gel chromatography that demonstrated a two-polypeptide subunit composition. Treatment of antigen E with 1% SDS (in the absence of reducing agent) resulted in the dissociation of the two polypeptide chains, which indicates that the bonds bridging the subunits are non-covalent in nature.

Low Molecular Weight Trypsin-Plasmin Inhibitors Isolated from Papain Treated Urinary Trypsin Inhibitor

1982 ◽  
Vol 47 (01) ◽  
pp. 014-018 ◽  
Author(s):  
H Sumi ◽  
N Toki ◽  
S Takasugi ◽  
S Maehara ◽  
M Maruyama ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Chromatography ◽  
Urinary Trypsin Inhibitor ◽  
Plasmin Activity ◽  
Molecular Weights ◽  
Plasmin Inhibitors

SummaryPapain treatment of human urinary trypsin inhibitor (UTI67; mol. wt. 43,000 by SDS-polyacrylamide gel electrophoresis, specific activity 1,897 U/mg protein) produced four new protease inhibitors, which were highly purified by gel chromatography on Sephadex G-100 and isoelectric focusing. The purified inhibitors (UTI26, UTI9-I, UTI9-II, and UTI9-III) were shown to be homogeneous by polyacrylamide disc gel electrophoresis, and had apparent molecular weights of 26,000, 9,000, 9,000, and 9,800, respectively, by sodium dodecyl sulfate gel electrophoresis. During enzymatic degradation of UTI67, the amino acid compositions changed to more basic, and the isoelectric point increased from pH 2.0 (UTI67) to pHs 4.4, 5.2, 6.6, and 8.3 (UTI26, UTI9-I, UTI9-II, and UTI9-III), respectively. Both the parent and degraded inhibitors had anti-plasmin activity as well as antitrypsin and anti-chymotrypsin activities. Much higher anti-plasmin/anti-trypsin and anti-plasmin/anti-chymotrypsin activities were observed in the degraded inhibitors than in the parent UTI67. They competitively inhibited human plasmin with Ki values of 1.13 X 10-7 - 2.12 X 10-6 M (H-D-Val-Leu-Lys-pNA substrate). The reactions were very fast and the active site of the inhibitors to plasmin was thought to be different from that to trypsin or chymotrypsin.

Partial characterization of an abnormal lactate dehydrogenase isoenzyme, LDH-1ex, in serum from a patient with hepatocellular carcinoma.

1989 ◽  
Vol 35 (5) ◽  
pp. 844-848
Author(s):  
D L Kalpaxis ◽  
E E Giannoulaki
Keyword(s):  
Hepatocellular Carcinoma ◽  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Chromatography ◽  
Heat Stable ◽  
Single Polypeptide ◽  
Polypeptide Chains

Abstract Serum from a patient with hepatocellular carcinoma contained an abnormal isoenzyme of lactate dehydrogenase (LDH; EC 1.1.1.27), LDH-1ex, that on electrophoresis on 10-g/L agarose gel migrated anodally to the LDH-1 band. This isoenzyme was partly purified by ultrafiltration and preparative electrophoresis. Gel chromatography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis studies of the resulting LDH-1ex preparation suggested that this isoenzyme is probably a tetramer made up of four single polypeptide chains (monomers), each having a molecular mass of about 32,000 Da. LDH-1ex was heat stable and reacted more readily with 2-hydroxybutyrate than did the slower migrating LDH-4 and LDH-5 isoenzymes. LDH-1ex showed no activity when lactate was omitted from the substrate solution or replaced by ethanol.

Urease. X. A study by gel electrophoresis of its dissociation by sodium dodecyl sulfate

1969 ◽  
Vol 47 (10) ◽  
pp. 989-991 ◽  
Author(s):  
D. P. Blattler ◽  
George Gorin
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Disulfide Bonds ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Dodecyl Sulfate ◽  
Polypeptide Chains

Urease, m.w. 480 000, treated with an excess of sodium dodecyl sulfate is converted to a product of greatly increased mobility in polyacrylamide gel electrophoresis. We estimate its weight to be about 80 000. Treatment with excess thiol and detergent yielded the same product as detergent alone, indicating that the subunit or subunits do not contain polypeptide chains linked by disulfide bonds.

Protein composition of Methanococcus thermolithotrophicus flagella

1992 ◽  
Vol 38 (11) ◽  
pp. 1162-1166 ◽  
Author(s):  
Alla S. Kostyukova ◽  
Georgi M. Gongadze ◽  
Anna Ya. Obraztsova ◽  
Konstantin S. Laurinavichus ◽  
Oleg V. Fedorov
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Key Words ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
Complete Removal ◽  
Methanococcus Thermolithotrophicus ◽  
Molecular Weights ◽  
Dodecyl Sulfate

Sodium dodecyl sulfate – polyacrylamide gel electrophoresis of flagella from the thermophilic methanogen Methanococcus thermolithotrophicus indicated that they were composed of three major proteins, with molecular weights of 62 000,44 000, and 26 000, whereas all previously studied flagella of mesophilic methanogens consisted of two subunits. Proteins were isolated by preparative electrophoresis followed by complete removal of sodium dodecyl sulfate and their renaturation. It was shown that at least two of the proteins contain a thermostable domain whose complete denaturation proceeds only upon prolonged boiling in the presence of sodium dodecyl sulfate. Key words: flagellin, thermostability, archaebacteria, Methanococcus thermolithotrophicus.

scholarly journals Lyt-2 glycoprotein is synthesized as a single molecular species.

1983 ◽  
Vol 157 (1) ◽  
pp. 365-370 ◽  
Author(s):  
E Rothenberg ◽  
D Triglia
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Cell Surface ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Two Dimensional ◽  
Post Translational Modification ◽  
Molecular Weights ◽  
Gradient Electrophoresis ◽  
Isoelectric Points

We investigated the possibility that the Lyt-2 molecules made by uncloned mouse T lymphocytes would show variable primary structures like those of immunoglobulins. Newly synthesized Lyt-2/3 complexes were found to include only two major components, both discrete glycoproteins with apparent molecular weights of 31,000 (31 K) and 35,000 (35 K). When products of Lyt-2.1 and Lyt-2.2 thymocytes were compared by two-dimensional nonequilibrium pH gradient electrophoresis and sodium dodecyl sulfate polyacrylamide gel electrophoresis, the isoelectric points of the 35 K molecules were different; thus, the 35 K component was likely to be encoded by the Lyt-2 locus itself. However, the 35 K molecules made by any one genotype were homogeneous in charge as well as in size. The homogeneity was obscured rapidly by post-translational modification. Most strikingly, within 30 min of initial synthesis, these processing events generated the conspicuous array of microheterogeneous products that form the "38 K" component of cell-surface Lyt-2/3.

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