What question did this study set out to answer?

Identify and purify the specific protein factor sensitive to N-ethylmaleimide that is required for vesicular transport between Golgi compartments.

November 1, 1988Proceedings of the National Academy of SciencesOpen Access

Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport.

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Identify and purify the specific protein factor sensitive to N-ethylmaleimide that is required for vesicular transport between Golgi compartments.
Established a cell-free complementation assay measuring intercisternal protein transport across Golgi compartments.
Inactivated Golgi membranes with N-ethylmaleimide (NEM) and assayed transport restoration upon adding fractionated cytosol.
Purified the functional complementation activity, designated NEM-sensitive factor (NSF), to homogeneity from cytosolic fractions.
Identified NSF as a tetramer composed of 76-kDa subunits that acts catalytically to mediate the transport of multiple vesicles.

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Implication

In vitro biochemical study reveals that N-ethylmaleimide-sensitive factor is a 76-kDa tetrameric protein in a cell-free Golgi system, indicating it acts catalytically during vesicular transport.

Cite This Study

Block et al. (1988) studied this question.

synapsesocial.com/papers/6a1bc59c26cb5670aa9cda13 https://doi.org/10.1073/pnas.85.21.7852

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Implication

In vitro biochemical study reveals that N-ethylmaleimide-sensitive factor is a 76-kDa tetrameric protein in a cell-free Golgi system, indicating it acts catalytically during vesicular transport.

Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport.

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Discussion

Implication

Cite This Study

Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport.

Key Points

Discussion

Implication

Cite This Study

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