What question did this study set out to answer?

To establish a sensitive, quantitative protein-chemical procedure for identifying and measuring actin isoforms directly from whole cellular extracts without requiring prior protein purification.

January 1, 1981European Journal of BiochemistryOpen Access

Actin Typing on Total Cellular Extracts

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Authors

JVJoël VandekerckhoveGhent University KWKlaus WeberUniversity of Geneva

Discussion

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Implication

Methodological study demonstrates sensitive, direct actin typing in total cellular extracts, indicating a reliable approach for quantifying actin isoforms without prior purification.

Key Points

To establish a sensitive, quantitative protein-chemical procedure for identifying and measuring actin isoforms directly from whole cellular extracts without requiring prior protein purification.
Targeted the amino-terminal tryptic peptide of actin as a specific divergence marker using non-radioactive protein-chemical analysis.
Tested the assay on total cellular extracts without preliminary fractionation, evaluating warm-blooded vertebrate tissues and Schneider L-2 Drosophila melanogaster cells at routine inputs of 10^5 cells.
Unambiguously distinguished six distinct vertebrate actin isoforms and directly measured the relative ratios of different actins within unpurified specimens.
Successfully predicted partial amino acid sequences of amino-terminal tryptic peptides, enabling accurate correlation with cloned DNA sequences in Drosophila melanogaster.

Cite This Study

Vandekerckhove et al. (1981) studied this question.

synapsesocial.com/papers/6a0dabc668ddba849a09d30d https://doi.org/10.1111/j.1432-1033.1981.tb05104.x

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January 1, 1981European Journal of BiochemistryOpen Access

Actin Typing on Total Cellular Extracts

View Full Paper

Ask AI

Bookmark

Authors

JVJoël VandekerckhoveGhent University KWKlaus WeberUniversity of Geneva

Discussion

Member takes

Implication

Methodological study demonstrates sensitive, direct actin typing in total cellular extracts, indicating a reliable approach for quantifying actin isoforms without prior purification.

Key Points

To establish a sensitive, quantitative protein-chemical procedure for identifying and measuring actin isoforms directly from whole cellular extracts without requiring prior protein purification.
Targeted the amino-terminal tryptic peptide of actin as a specific divergence marker using non-radioactive protein-chemical analysis.
Tested the assay on total cellular extracts without preliminary fractionation, evaluating warm-blooded vertebrate tissues and Schneider L-2 Drosophila melanogaster cells at routine inputs of 10^5 cells.
Unambiguously distinguished six distinct vertebrate actin isoforms and directly measured the relative ratios of different actins within unpurified specimens.
Successfully predicted partial amino acid sequences of amino-terminal tryptic peptides, enabling accurate correlation with cloned DNA sequences in Drosophila melanogaster.

Cite This Study

Vandekerckhove et al. (1981) studied this question.

synapsesocial.com/papers/6a0dabc668ddba849a09d30d https://doi.org/10.1111/j.1432-1033.1981.tb05104.x

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