Isolation and purification of myelin proteolipid protein using high speed gel filtration in sodium dodecyl sulfate

1985 ◽  
Vol 10 (6) ◽  
pp. 865-869 ◽  
Author(s):  
John L. Trotter ◽  
Cindy L. Wegescheide
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
High Speed ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Proteolipid Protein ◽  
Myelin Proteolipid Protein ◽  
Isolation And Purification ◽  
Dodecyl Sulfate ◽  
Myelin Proteolipid

High-Speed Gel Filtration of Polypeptides in Sodium Dodecyl Sulfate

1979 ◽  
Vol 86 (3) ◽  
pp. 639-642 ◽  
Author(s):  
Takeyoshi IMAMURA ◽  
Kazue KONISHI ◽  
Masao YOKOYAMA ◽  
Katsutoshi KONISHI
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
High Speed ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Dodecyl Sulfate

Rat lingual lipase: partial purification, hydrolytic properties, and comparison with pancreatic lipase

1984 ◽  
Vol 247 (4) ◽  
pp. G385-G393 ◽  
Author(s):  
I. M. Roberts ◽  
R. K. Montgomery ◽  
M. C. Carey
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Pancreatic Lipase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Hydrolytic Activity ◽  
Partial Purification ◽  
Ph Optimum ◽  
Dodecyl Sulfate ◽  
Triton X

We have partially purified lingual lipase from the serous glands of rat tongue. With a combination of Triton X-100 extraction or Triton X-114 phase-separation techniques, Bio-Bead SM-2 treatment, dialysis, and gel filtration on Sephadex G-200 or Sephacryl S-300, we obtained a sparingly soluble lipid-free protein demonstrating hydrolytic activity against triglycerides and negligible phospholipase or cholesteryl esterase activities. Compared with homogenate, specific activities of the enzyme were enriched 3- to 5-fold prior to gel filtration and 10-fold after gel filtration. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration under denaturing conditions (6 M guanidine X HCl or 0.1% sodium dodecyl sulfate) revealed one major glycoprotein band with Mr approximately 50,000. Gel filtration of the active enzyme in 0.1% Triton X-100 gave an Mr approximately 270,000-300,000, suggesting extensive self-aggregation. With both tributyrin and triolein, the pH optimum of the purified enzyme was 4.0 and activity extended from pH 2.0 to 8.0. In contrast to purified human pancreatic lipase, lingual lipase hydrolyzed triglyceride emulsions and mixed micelles stabilized with both short-chain (dihexanoyl) and long-chain (egg) lecithin and were inhibited only slightly (18-25%) by micellar concentrations of two common bile salts, taurodeoxycholate and taurocholate. Our results suggest that the hydrolysis of dietary fat by lingual lipase may extend from the pharynx through the esophagus and stomach and into the upper small intestine.

scholarly journals Denaturant-induced stimulation of the beta-migrating plasminogen activator inhibitor in endothelial cells and serum

Blood ◽  
1986 ◽  
Vol 68 (6) ◽  
pp. 1298-1305 ◽  
Author(s):  
LA Erickson ◽  
CM Hekman ◽  
DJ Loskutoff
Keyword(s):  
Endothelial Cells ◽  
Sodium Dodecyl Sulfate ◽  
Human Serum ◽  
Plasminogen Activator ◽  
Serum Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Zone Electrophoresis ◽  
Dodecyl Sulfate

Cultured bovine aortic endothelial cells and human serum contain plasminogen activator inhibitors (PAIs) that are immunologically related. In the present study, the electrophoretic mobilities, molecular weights (mol wt), and activities of these PAIs were compared. When fractionated by agarose zone electrophoresis, both PAIs migrated with beta mobility as compared with the mobilities of human plasma/serum proteins. Two-dimensional electrophoretic analysis, employing agarose zone electrophoresis in the first dimension and sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the second dimension, indicated that these beta-PAIs comigrated, both having a mol wt of approximately 50,000. The activity of the PAI in endothelial cell- conditioned medium is enhanced severalfold by treatment with either sodium dodecyl sulfate or guanidine. In preliminary experiments, we were unable to stimulate the PAI activity of undiluted serum by similar treatments. However, the PAI activities in both diluted serum and gel- filtered or electrophoretically fractionated serum were enhanced by treatment with these denaturants. The gel filtration studies also revealed that serum contains multiple forms of the beta-PAI. These forms may represent polymeric PAI and/or complexes between the PAI and other serum components. These findings indicate that the primary PAIs in bovine endothelial cells and human serum are not only immunologically related but are also biochemically similar.

scholarly journals Studies of the Interaction of Poly(ethylene oxide) with Sodium Dodecyl Sulfate by Gel Filtration

1980 ◽  
Vol 53 (7) ◽  
pp. 1864-1866 ◽  
Author(s):  
Tsunetaka Sasaki ◽  
Kaoru Kushima ◽  
Kazunori Matsuda ◽  
Hitoshi Suzuki
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Ethylene Oxide ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Dodecyl Sulfate ◽  
Poly Ethylene Oxide ◽  
Poly Ethylene
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