The passage of heterologous serum proteins from the circulation into the ovum of the fowl

Knight, Patricia F.; Schechtman, A. M.

doi:10.1002/jez.1401270205

Cited by 57 publications

(14 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Both morphological and physiological analyses have established that an important aspect of yolk formation in animal oocytes is the uptake of protein from the Mood. Fine structural configurations consistent with intensive pinocytotic activity are seen during periods of rapid yolk formation in oocytes of amphibians (8,29), chickens (22), and a variety of insects (1,4,9,19,21), and the sequestering of specific blood proteins in yolk bodies has been demonstrated experimentally in the chicken (11) and in moths (24). This paper attempts to extend these observations by describing an electron microscope analysis of the ovary of the cecropia moth, Hyalophora cecropia (L.).…”

mentioning

confidence: 83%

Protein Uptake in the Oocytes of the Cecropia Moth

Stay

1965

The Journal of Cell Biology

153

View full text Add to dashboard Cite

The formation of yolk spheres in the oocyte of the cecropia moth, Hyalophora cecropia (L.), is known immunologically to result largely from uptake of a sex-limited blood protein.Recent electron microscope analyses of insect and other animal oocytes have demonstrated fine structural configurations consistent with uptake of proteins by pinocytosis. An electron microscope analysis of the cecropia ovary confirms the presence of similar structural modifications. With the exception of two apparently amorphous layers, the basement lamella on the outer surface of the follicular epithelium and the vitelline membrane on the inner, there is free access of blood to the oocyte surface between follicle cells. Dense material is found in the interfollicular cell space and adsorbed to the outer surface of the much folded oocyte membrane. Pits in the oocyte membrane and vesicles immediately under it are lined with the same dense material not unlike the yolk spheres in appearance. Introduction of ferritin into the blood of a developing cecropia moth and its localization adsorbed to the surface of the oocyte, and within the vesicles and yolk spheres of the oocyte cortex, is experimental evidence that the structural modifications of the oocyte cortex represent stages in the pinocytosis of blood proteins which arrive at the oocyte surface largely by an intercellular route. Small tubules attached to the yolk spheres are provisionally interpreted as a manifestation of oocyte-synthesized protein being contributed to the yolk spheres.

show abstract

mentioning

confidence: 83%

Protein Uptake in the Oocytes of the Cecropia Moth

Stay

1965

The Journal of Cell Biology

153

View full text Add to dashboard Cite

show abstract

“…The antibody is in the water-soluble or livetin fraction of the yolk proteins (Jukes, Fraser & Orr, 1934) and this fraction is immunologically indistinguishable from serum globulin (Jukes & Kay, 1932), being electrophoretically separable into the same three components (Shepard & Hottle, 1949). Antibody appears in the yolk unaltered and is not precipitable in the livetin fraction when immune serum from another species is administered intravenously to the laying hen (Knight & Schechtman, 1954). The antibody persists in the yolk and the concentration does not seem to be reduced during incubation or even after hatching so long as any yolk remains (Brierley & Hemmings, 1956).…”

Section: (I) Transmission To the Chickmentioning

confidence: 99%

The Passive Immunity of the Young Mammal

Brambell¹

1958

Biological Reviews

306

View full text Add to dashboard Cite

“…The buffers used were either ( a ) veronal buffer, pH 8.6, p = 0.05 (1:1), or (b) veronal -sodium acetate buffer pH 8.6, p = 0.07 (15).…”

Section: Filter Paper Electroptzoresismentioning

confidence: 99%

Studies on the Livetins of Hen's Egg Yolk: I. Identification of Paper-Electrophoretic and Immunoelectro-Phoretic Livetin Fractions With Serum Protein Antigens by Immunoelectrophoretic Analysis

Mok¹,

Common²

1964

Can. J. Biochem.

View full text Add to dashboard Cite

Immunoelectrophoretic analysis of a n egg yolk livetin preparation has demonstrated the presence of six distinct fractions, which were numbered 1, 2, 3, 4, 5, a n d 6 from the anodic end of the electropherogram. Four of these fractions have been identified with four livetin fractions obtained by paper electrophoresis a s follows: immunoelectrophoretic fraction 1 with alpha-livetin, fraction 2 with beta-livetin, fraction 4 with gammal-livetin, and fraction 5 with gammaz-livetin.Immunoelectrophoresis of hen serum or cock serum against antilivetin serum has shown t h a t both hen a n d cock sera contain antigens electrophoretically and immunologically identical t o alpha-, beta-, gammal-, and gammaz-livetins.'Macdonald College Journal Series No. 502.

show abstract

The passage of heterologous serum proteins from the circulation into the ovum of the fowl

Cited by 57 publications

References 29 publications

Protein Uptake in the Oocytes of the Cecropia Moth

Protein Uptake in the Oocytes of the Cecropia Moth

The Passive Immunity of the Young Mammal

Studies on the Livetins of Hen's Egg Yolk: I. Identification of Paper-Electrophoretic and Immunoelectro-Phoretic Livetin Fractions With Serum Protein Antigens by Immunoelectrophoretic Analysis

Contact Info

Product

Resources

About