Differential Uptake of Fluorescent-Tagged Low Density Lipoprotein by Cells from the Primate Corpus Luteum: Isolation and Characterization of Subtypes of Small and Large Luteal Cells*

Endocrinology ◽  
1991 ◽  
Vol 129 (6) ◽  
pp. 3247-3253 ◽  
Author(s):  
JOHN D. BRANNIAN ◽  
STANLEY M. SHIIGI ◽  
RICHARD L. STOUFFER
Biochimie ◽  
1986 ◽  
Vol 68 (4) ◽  
pp. 531-541 ◽  
Author(s):  
Lawrence P. Aggerbeck ◽  
François Caron ◽  
Nicole Lachacinski ◽  
Marie-Elisabeth Bouma

1968 ◽  
Vol 46 (8) ◽  
pp. 983-988 ◽  
Author(s):  
J. Z. Augustyniak ◽  
W. G. Martin

Two glycopeptides (A and B) were isolated from pronase-digested vitellenin, the protein moiety of the low-density lipoprotein of hen's egg yolk. Aspartic acid was the only N-terminal amino acid of both glycopeptides but only A contained N-acetylneuraminic acid. A contained 55% hexose (mannose), 14% hexosamine, 12% N-acetylneuraminic acid, 0.71% amide nitrogen, and its molecular weight was 2.3 × 103. The corresponding values for B were 64, 17, 0.0, 0.75, and 2.0 × 103. Chemical analyses showed that B (and probably A) occurs in vitellenin with the heteropolysaccharide group bound N-glycosidically via the β-amide group of an asparaginyl residue. The indicated structure is R∙(NH)Asp∙Thr∙Ser∙(Ala, Gly, Val)∙Ile, where R, the heteropolysaccharide group, contains 2 hexosamine and 8 hexose residues.


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