scholarly journals Studies in immunochemistry. 16. The isolation of blood-group active mucoids from ovarian cyst fluids*

1955 ◽  
Vol 60 (3) ◽  
pp. 428-436 ◽  
Author(s):  
R. A. Gibbons ◽  
W. T. J. Morgan ◽  
Marion Gibbons
Keyword(s):  
Blood Group ◽  
Ovarian Cyst ◽  
Cyst Fluids

Placental Protein 5 in Benign and Malignant Ovarian Cyst Fluids

Tumor Biology ◽  
1987 ◽  
Vol 8 (4) ◽  
pp. 230-232 ◽  
Author(s):  
Gábor Than ◽  
Markku Seppälä ◽  
Imre Csaba ◽  
Koichi Iino ◽  
Volkert Briese
Keyword(s):  
Ovarian Cyst ◽  
Placental Protein ◽  
Cyst Fluids

Luteinizing hormone in peritoneal and ovarian cyst fluids: a predictor of ovarian carcinoma

2003 ◽  
Vol 110 (2) ◽  
pp. 207-210 ◽  
Author(s):  
R Halperin ◽  
M Pansky ◽  
Z Vaknin ◽  
S Zehavi ◽  
I Bukovsky ◽  
...  
Keyword(s):  
Luteinizing Hormone ◽  
Ovarian Carcinoma ◽  
Ovarian Cyst ◽  
Cyst Fluids

scholarly journals Partial deglycosylation of blood-group-specific glycoproteins

1980 ◽  
Vol 185 (2) ◽  
pp. 327-337 ◽  
Author(s):  
A S R Donald
Keyword(s):  
Acetic Acid ◽  
Amino Acid ◽  
Blood Group ◽  
Time Course ◽  
Gel Filtration ◽  
Lumbricus Terrestris ◽  
Exchange Chromatography ◽  
Acid Reagent ◽  
Almost All ◽  
Cyst Fluids

The time course for the partial deglycosylation of blood-group-specific glycoproteins from human ovarian-cyst fluids with 0.25 M-H2SO4/acetic acid and 6 M-HCl in methanol was studied. Either reagent readily removed about 80% of the carbohydrate from the glycoproteins to leave non-diffusible glycopeptides that contain N-acetylgalactosamine as the predominant sugar. Some changes in amino acid distribution were observed during the deglycosylation, which were attributed to an accelerated break-up of the nonglycosylated regions of the parent glycoprotein. The N-acetylgalactosaminyl-peptides isolated were judged to be polydisperse by gel filtration, and ion-exchange chromatography divided the glycopeptide population into several fractions with differing amino acid compositions. A Lumbricus terrestris hexosaminidase preparation was successful in removing almost all the remaining sugar from the glycopeptides, but caused further rupture of the peptide. When a per O-acetylated glycoprotein was treated with the H2SO4/acetic acid reagent the glycopeptide contained, in addition to N-acetylgalactosamine, about 50% of the sialic acid present in the parent glycoprotein, indicating that most of this sugar is located near the peptide end of the carbohydrate chains.

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