Formaldehyde and ribosomal conformation

Moshe Tal

doi:10.1016/0005-2787(70)90579-4

Formaldehyde and ribosomal conformation

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Abstract

The effect of formaldehyde on ribosomal conformation was investigated spectrophotometrically and viscometrically. Thermal denaturation of ribosomes dissolved in 1 mM sodium acetate (pH 7.4) in the presence of formaldehyde results in: 1. (1) A decrease in the melting temperature (T_m), from 63° in the absence of formaldehyde, down to 51° in the presence of 9.4 % reagent. 2. (2) Irreversibility of the hyperchromicity upon cooling. 3. (3) Shift of λ_max from 257 to 262 nm. Viscometric measurements in the presence of formaldehyde at different temperatures revealed no changes in specific viscosity (η_sp), due to fixation. Parallel experiments with ribosomes and ribosomal RNA where η_sp was measured at different formaldehyde concentrations, show that the presence of ribosomal proteins attached to the rRNA, increases the fixation markedly compared with free rRNA. The η_sp values of rRNA at high temperatures decrease gradually with increasing formaldehyde concentration. Due to the fixation, the high η_sp value of rRNA obtained at high temperature is retained on cooling.

Original language	English
Pages (from-to)	470-476
Number of pages	7
Journal	BBA Section Nucleic Acids And Protein Synthesis
Volume	224
Issue number	2
DOIs	https://doi.org/10.1016/0005-2787(70)90579-4
State	Published - 14 Dec 1970
Externally published	Yes

ASJC Scopus subject areas

Medicine (all)

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10.1016/0005-2787(70)90579-4

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title = "Formaldehyde and ribosomal conformation",

abstract = "The effect of formaldehyde on ribosomal conformation was investigated spectrophotometrically and viscometrically. Thermal denaturation of ribosomes dissolved in 1 mM sodium acetate (pH 7.4) in the presence of formaldehyde results in: 1. (1) A decrease in the melting temperature (Tm), from 63° in the absence of formaldehyde, down to 51° in the presence of 9.4 % reagent. 2. (2) Irreversibility of the hyperchromicity upon cooling. 3. (3) Shift of λmax from 257 to 262 nm. Viscometric measurements in the presence of formaldehyde at different temperatures revealed no changes in specific viscosity (ηsp), due to fixation. Parallel experiments with ribosomes and ribosomal RNA where ηsp was measured at different formaldehyde concentrations, show that the presence of ribosomal proteins attached to the rRNA, increases the fixation markedly compared with free rRNA. The ηsp values of rRNA at high temperatures decrease gradually with increasing formaldehyde concentration. Due to the fixation, the high ηsp value of rRNA obtained at high temperature is retained on cooling.",

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T1 - Formaldehyde and ribosomal conformation

AU - Tal, Moshe

PY - 1970/12/14

Y1 - 1970/12/14

N2 - The effect of formaldehyde on ribosomal conformation was investigated spectrophotometrically and viscometrically. Thermal denaturation of ribosomes dissolved in 1 mM sodium acetate (pH 7.4) in the presence of formaldehyde results in: 1. (1) A decrease in the melting temperature (Tm), from 63° in the absence of formaldehyde, down to 51° in the presence of 9.4 % reagent. 2. (2) Irreversibility of the hyperchromicity upon cooling. 3. (3) Shift of λmax from 257 to 262 nm. Viscometric measurements in the presence of formaldehyde at different temperatures revealed no changes in specific viscosity (ηsp), due to fixation. Parallel experiments with ribosomes and ribosomal RNA where ηsp was measured at different formaldehyde concentrations, show that the presence of ribosomal proteins attached to the rRNA, increases the fixation markedly compared with free rRNA. The ηsp values of rRNA at high temperatures decrease gradually with increasing formaldehyde concentration. Due to the fixation, the high ηsp value of rRNA obtained at high temperature is retained on cooling.

AB - The effect of formaldehyde on ribosomal conformation was investigated spectrophotometrically and viscometrically. Thermal denaturation of ribosomes dissolved in 1 mM sodium acetate (pH 7.4) in the presence of formaldehyde results in: 1. (1) A decrease in the melting temperature (Tm), from 63° in the absence of formaldehyde, down to 51° in the presence of 9.4 % reagent. 2. (2) Irreversibility of the hyperchromicity upon cooling. 3. (3) Shift of λmax from 257 to 262 nm. Viscometric measurements in the presence of formaldehyde at different temperatures revealed no changes in specific viscosity (ηsp), due to fixation. Parallel experiments with ribosomes and ribosomal RNA where ηsp was measured at different formaldehyde concentrations, show that the presence of ribosomal proteins attached to the rRNA, increases the fixation markedly compared with free rRNA. The ηsp values of rRNA at high temperatures decrease gradually with increasing formaldehyde concentration. Due to the fixation, the high ηsp value of rRNA obtained at high temperature is retained on cooling.

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DO - 10.1016/0005-2787(70)90579-4

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Formaldehyde and ribosomal conformation

Abstract

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