# MECHANISMS OF ACTION OF CHOLERA TOXIN

> **NIH NIH R01** · TUFTS UNIVERSITY BOSTON · 1990 · $133,162

## Abstract

Cholera toxin in vitro catalyses the transfer of ADP-ribose from NAD ion to a
number of cellular proteins.  These are a) 42K, somtimes 50K, which are
regulatory components of adenylate cyclase, b) often 98K, 23K, which share
sequences with 42K but whose nature isn't clear, c) even more minor components
that have not been studied at all.
In the coming year we shall continue to study the minor components, especially
98K, to determine its physiological function and the possible change of function
upon ADP-ribosylation.  We shall use erythrocytes and enterocytes.

We shall also examine non-vertebrate tissues to see what targets, if any, they
have, what their sizes are, when they arose, or changed size, and how these
changes relate to the evolution of adenylate cyclase and its regulatory systems.

## Key facts

- **NIH application ID:** 3126902
- **Project number:** 5R01AI016928-12
- **Recipient organization:** TUFTS UNIVERSITY BOSTON
- **SAM.gov UEI:** C1F5LNUF7W86
- **Principal Investigator:** ARTHUR M. DONOHUE-ROLFE
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1990
- **Award amount:** $133,162
- **Award type:** 5
- **Project period:** 1979-09-01 → 1991-05-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3126902

## Citation

> US National Institutes of Health, RePORTER application 3126902, MECHANISMS OF ACTION OF CHOLERA TOXIN (5R01AI016928-12). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3126902. Licensed CC0.

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