The protection of ram and bull spermatozoa by the low density lipoprotein fraction of egg yolk during storage at 5°C and deep-freezing

A study was made of the action of phosphatidase D (phospholipase D) from Clostridium perfringens (C. welchii) on five constituents of the yolk of hens' eggs (α- and β-lipovitellin, the low-density lipoprotein fraction, granules, and lecithin) in aqueous solution, in the absence and presence of chloroform. Although the untreated lipovitellins were little affected by the enzyme, after absorption of chloroform, a large proportion of their phospholipids was hydrolyzed. In this respect they resembled lecithin but differed from the low-density yolk lipoproteins, whose phospholipids were rapidly hydrolyzed by the enzyme in the presence or absence of chloroform. The mechanism of this type of chloroform activation is discussed.

Download Full-text

THE ACTION OF CLOSTRIDIUM PERFRINGENS PHOSPHATIDASE ON THE LIPOVITELLINS AND OTHER EGG YOLK CONSTITUENTS

Canadian Journal of Biochemistry and Physiology ◽

10.1139/y63-049 ◽

1963 ◽

Vol 41 (1) ◽

pp. 409-416 ◽

Cited By ~ 1

Author(s):

R. W. Burley ◽

D. J. Kushner

Keyword(s):

Aqueous Solution ◽

Clostridium Perfringens ◽

Phospholipase D ◽

Low Density Lipoprotein ◽

Density Lipoprotein ◽

Egg Yolk ◽

Lipoprotein Fraction ◽

Low Density

A study was made of the action of phosphatidase D (phospholipase D) from Clostridium perfringens (C. welchii) on five constituents of the yolk of hens' eggs (α- and β-lipovitellin, the low-density lipoprotein fraction, granules, and lecithin) in aqueous solution, in the absence and presence of chloroform. Although the untreated lipovitellins were little affected by the enzyme, after absorption of chloroform, a large proportion of their phospholipids was hydrolyzed. In this respect they resembled lecithin but differed from the low-density yolk lipoproteins, whose phospholipids were rapidly hydrolyzed by the enzyme in the presence or absence of chloroform. The mechanism of this type of chloroform activation is discussed.

Download Full-text

Characterization of glycopeptides derived from the low-density lipoprotein of hen's egg yolk

Canadian Journal of Biochemistry ◽

10.1139/o68-147 ◽

1968 ◽

Vol 46 (8) ◽

pp. 983-988 ◽

Cited By ~ 6

Author(s):

J. Z. Augustyniak ◽

W. G. Martin

Keyword(s):

Low Density Lipoprotein ◽

Density Lipoprotein ◽

Egg Yolk ◽

Low Density ◽

Amide Nitrogen ◽

Acetylneuraminic Acid ◽

Hen’S Egg ◽

Terminal Amino ◽

Protein Moiety

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.

Download Full-text