Preparation and Characterization of Mammalian Plasma Membranes

1979 ◽  
Vol 7 (6) ◽  
pp. 1328-1328
Author(s):  
C. LOVELIDGE
Keyword(s):  
Plasma Membranes

scholarly journals Characterization of cobalamin receptor sites in brush-border plasma membranes of the tapeworm Spirometra mansonoides.

1983 ◽  
Vol 258 (7) ◽  
pp. 4261-4265
Author(s):  
P A Friedman ◽  
P P Weinstein ◽  
J F Mueller ◽  
R H Allen
Keyword(s):  
Brush Border ◽  
Plasma Membranes ◽  
Receptor Sites

scholarly journals Characterization of calcium binding to adipocyte plasma membranes.

1976 ◽  
Vol 251 (17) ◽  
pp. 5345-5351
Author(s):  
J M McDonald ◽  
D E Bruns ◽  
L Jarett
Keyword(s):  
Calcium Binding ◽  
Plasma Membranes ◽  
Adipocyte Plasma Membranes

scholarly journals Purification and characterization of a major glycoprotein in rat hepatoma plasma membranes. One of the membrane proteins released by phosphatidylinositol-specific phospholipase C

1987 ◽  
Vol 241 (1) ◽  
pp. 63-70 ◽  
Author(s):  
Y Ikehara ◽  
Y Hayashi ◽  
S Ogata ◽  
A Miki ◽  
T Kominami
Keyword(s):  
Alkaline Phosphatase ◽  
Phospholipase C ◽  
Plasma Membranes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Soluble Form ◽  
Microsomal Membranes ◽  
Hydrophobic Nature ◽  
Rat Hepatoma

A major glycoprotein of rat hepatoma plasma membranes was selectively released as a soluble form by incubating the membrane with phosphatidylinositol-specific phospholipase C. The soluble form corresponding to the glycoprotein was also prepared by butan-1-ol extraction of microsomal membranes at pH 5.5, whereas extraction at pH 8.5 yielded an electrophoretically different form with a hydrophobic nature. The soluble glycoprotein extracted at pH 5.5 was purified by sequential chromatography on concanavalin A-Sepharose, Sephacryl S-300 and anti-(alkaline phosphatase) IgG-Sepharose, the last step being used to remove a contaminating alkaline phosphatase. The glycoprotein thus purified was a single protein with Mr 130,000 in SDS/polyacrylamide-gel electrophoresis, although it behaved as a dimer in gel filtration on Sephacryl S-300. The glycoprotein was analysed for amino acid and carbohydrate composition. The composition of the carbohydrate moiety, which amounted to 64% by weight, suggested that the glycoprotein contained much larger numbers of N-linked oligosaccharide chains than those with O-linkage. It was confirmed that the purified glycoprotein was immunologically identical not only with that released by the phospholipase C but also with the hydrophobic form extracted with butan-1-ol at pH 8.5. The results indicate that the glycoprotein of rat hepatoma plasma membranes, which has an unusually high content of carbohydrate, is another membrane protein released by phosphatidylinositol-specific phospholipase C, as documented for alkaline phosphatase, acetylcholinesterase and Thy-1 antigen.

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