5a !?ALSlEIL-TlIE EFFEOT OF SALTS 0s DETEROESCE [Ysrclr, 1041 ketol group in respect to osnzone fornintion is very different in t,lie two compounds. Actioii of ll'tjs' so?iition.-After some defuiite nmount of absorption, the contents of the renction vessel were trnnsferred to a 500-C.C. glass-stoppe
The effects of detergents on the polymerization properties of actin
✍ Scribed by Kinga Ujfalusi-Pozsonyi; Gábor Hild; Pál Gróf; Zsuzsanna Gutay-Tóth; Zsolt Bacsó; Miklós Nyitrai
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 427 KB
- Volume
- 9999A
- Category
- Article
- ISSN
- 0196-4763
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
for inucli cnrefiil esperiineiitnl work, nntl to the Council of tlie Wool Industries Rcsenrclt Associntiou for permission to publish this piqJCr. Wool Industries Resenrcli Aswcintion, f Icntlinglcy, r.eetis Ilecel%-xl Jau. 25, 1Ok1
The G-F transformation of actin was studied in terms of a n interaction between different counterions and actin niacroion by means of electrometric measurements. Due to the polyelectrolyte structure of the actin molecule, the electrostatic interactions must play a predominant role. In this sense the
We report on how physiological concentrations of capping protein shorten actin filaments and on the remarkably fluid nature of solutions of such short filaments even at the high concentrations that exist in cells. We measured the lengths of actin filaments formed by spontaneous polymerization of hig