ISSN:
1432-2048
Keywords:
Glucan synthase
;
Golgi apparatus
;
Inosine diphosphatase
;
Pisum, secretory vesicles
;
Renografin gradient
;
Secretory vesicle
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract In homogenates of stem sections from etiolated pea (Pisum sativum L.) seedlings, secretory vesicles can be separated from Golgi-apparatus cisternae by rate-zonal centrifugation in renografin gradients. Optically, two bands of turbidity are observed, the uppermost containing the secretory vesicles and the lower one the Golgi-apparatus cisternae. The absence of glutaraldehyde in the homogenizing medium has allowed the effective characterization of marker-enzyme activities. Golgi-apparatus cisternae have been recognized by the presence of inosine-diphosphatase and glucan-synthase I activities as well as by electron microscopy. In contrast, although secretory vesicles also bear inosine diphosphatase they do not appear to possess glucan-synthase activity. Three plasma-membrane markers, NPA-binding, glucan synthase II, and KCl,Mg2+-adenosine triphosphatase (pH 6.5), were not detected in secretory vesicles. Pulse-chase experiments with [3H]glucose support our designation of secretory vesicles and Golgi-cisternal fractions.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00397244
Permalink