[59] Immunoadsorption of ovalbumin synthesizing polysomes and partial purification of ovalbumin messenger RNA

Schimke, Robert T.; Palacios, Rafael; Sullivan, Drew; Kiely, Mary L.; Gonzales, Carmen; Taylor, John M.

doi:10.1016/0076-6879(74)30061-4

Cited by 36 publications

(13 citation statements)

References 14 publications

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“…Nonimmune rabbit serum (2 ,ul) and goat anti-rabbit IgG antiserum (Miles) (20 ,ul) were added and incubation was continued for 12 hr. The immune complexes were collected and washed as described by Schimke et aL (22), with an Eppendorf centrifuge; radioactivity was determined with a gamma counter.…”

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confidence: 99%

Developmental regulation of secretory protein synthesis in rat seminal vesicle.

Kistler¹,

Ostrowski²,

Kistler³

1981

Proc. Natl. Acad. Sci. U.S.A.

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This paper reports a developmental study of one of the major secretory proteins (SVS IV) of the rat seminal vesicle. Measured by radioimmunoassay, SVS IV is detectable even in very young rats (5 days old) but does not begin to accumulate in massive amounts until animals reach about 35 days of age. We have compared SVS IV synthesis by minced tissue from rats undergoing sexual maturation (25-60 days of age) with levels of translatable SVS IV mRNA present. Between 25 and 60 days of age, the proportion of newly synthesized protein devoted to SVS IV by tissue minces increased from 0.8% to 20%. In contrast, the proportion of total RNA devoted to translatable SVS IV mRNA was already high in the immature glands and increased less than 4-fold during development. These results seem to indicate that factors other than the presence of potentially translatable message regulate the rate of net synthesis of SVS IV during seminal vesicle maturation.

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confidence: 99%

Developmental regulation of secretory protein synthesis in rat seminal vesicle.

Kistler¹,

Ostrowski²,

Kistler³

1981

Proc. Natl. Acad. Sci. U.S.A.

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“…At 24 h P1, cells grown on four 100-mm dishes were pulsed for 1 h with 500 iLCi of 32Pi per ml in phosphate-free Eagle medium. Polyribosomes were prepared from the cells by the method of Schimke (37). Briefly.…”

Section: Fig 3 Identification Of Phosphorylated Vp1 Associated Withmentioning

confidence: 99%

Synthesis, posttranslational modifications, and nuclear transport of polyomavirus major capsid protein VP1

Fattaey

Consigli

1989

J Virol

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Polyomavirus major capsid protein VP1 synthesis was studied in infected primary baby mouse kidney cells. A standard curve of VP1 protein was used to quantitate VP1 in the cytoplasm and nucleus of infected cells during the time course of infection. Polyomavirus VP1 continued to be accumulated in the cytoplasm of the cells until 27 h postinfection, at which time the synthesis of VP1 leveled off. VP1 continued to accumulate in the nucleus of the infected cells throughout the course of infection. The presence of the six isospecies, A to F, of polyomavirus VP1 was also studied to determine the relative quantity of each species during the time course of infection. All six species were found in the cytoplasm and nucleus of infected cells at various times postinfection. However, the relative quantity of each species was different at early as compared with later times of infection. In addition, phosphorylated VP1 was found in isolated polyribosomes of infected cells, suggesting that phosphorylation of VP1 is a cotranslational modification. Examination of the effect of macromolecular synthesis on the transport of VP1 into the nucleus of infected baby mouse kidney cells as well as the rate of its nuclear accumulation during and after protein synthesis inhibition revealed that the continual transport and accumulation of VP1 in the nucleus required protein synthesis.

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“…An immunoglobulin fraction was isolated from heat-inactivated (30 min at 56°C) rabbit anti-human lung ACE serum by two ammonium sulfate precipitations and carboxymethyl and DEAE-cellulose column chromatography (29).…”

Section: Methodsmentioning

confidence: 99%