## Abstract The presence of cytochalasin A inhibits the self‐assembly of beef brain tubulin and rabbit muscle G‐actin in vitro and also decreases the colchicine binding of tubulin. Prior reaction of cytochalasin A with 2‐mercaptoethanol destroys its inhibitory effects. It is shown that cytochalasin
In vivo and in vitro effect of cold on the degree of polymerization of tubulin in toad brain and testis
✍ Scribed by Lopez, Luis A. ;Bertini, Francisco
- Publisher
- John Wiley and Sons
- Year
- 1982
- Tongue
- English
- Weight
- 346 KB
- Volume
- 221
- Category
- Article
- ISSN
- 0022-104X
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
The tubulin of both brain and testis of the toad Bufo arenarum was partially depolymerized when the animals were maintained on ice for 90 minutes or 17 hours. Recovery of the animals at room temperature restored the normal degree of polymerization in both organs. Normalization of the polymerization degree also occurred in organs separated from cooled animals and incubated in vitro for 90 minutes at 20°C. When the organs were cooled in vitro, only testicular tubulin underwent depolymerization, and in a degree similar to that occurring by incubation at 20°C. The results suggest that the mechanisms regulating tubulin depolymerization in vivo are different from those taking place in vitro.
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