Name: Ecto-Atpases: Recent Progress on Structure and Function (en Inglés)
Price: 165103.00 COP
Availability: InStock
Author: Plesner, Liselotte ; Kirley, Terence L. ; Knowles, Aileen F.
ISBN: 9781461377290

portada Ecto-Atpases: Recent Progress on Structure and Function (en Inglés)

Ecto-Atpases: Recent Progress on Structure and Function (en Inglés)

Formato

Libro Físico

Editorial

Springer

Autor

Plesner, Liselotte ; Kirley, Terence L. ; Knowles, Aileen F.

Idioma

Inglés

N° páginas

294

Encuadernación

Tapa Blanda

Dimensiones

25.4 x 17.8 x 1.7 cm

Peso

0.54 kg.

ISBN13

9781461377290

Categorías

Fisiología
Patología
Bioquímica
Árboles, flores silvestres y plantas: interés general

Ecto-Atpases: Recent Progress on Structure and Function (en Inglés)

Plesner, Liselotte ; Kirley, Terence L. ; Knowles, Aileen F. (Autor) · Springer · Tapa Blanda

Libro Nuevo Importado

Envío: 14 a 20 días háb.

$ 330.205$ 165.103

-50%

Costos de importación incluídos en el precio ✅

Libro Nuevo

Quedan más de 100 unidades

$ 165.103

¡Envío Gratis! Llega entre el 05 Ago y el 18 Ago a Bogota, Cundinamarca. Seleccionar ubicación

Agregar a lista de deseos

Reseña del libro "Ecto-Atpases: Recent Progress on Structure and Function (en Inglés)"

It has been known for almost 50 years that many cells carry enzymes that hydro- lyze extracellular ATP, and the term "ecto-ATPase" was used first by Engelhardt 40 years ago. But until the end of the 1970's, the idea of an ATPase with its ATP hydrolyzing site on the outside of the cell membrane was met with substantial skepticism since it was thought that ATP was strictly intracellular. Nevertheless, ecto-ATPase activity was dem- onstrated using a variety of intact cells. Most ecto-ATPase(s) exhibited three common 2 characteristics: 1) activation by either Ca + or Mg2+, 2) insensitivity to the commonly used inhibitors ofF-type, P-type, and V-type ATPases, and 3) ability to hydrolyze nucleo- side triphosphates and often nucleoside diphosphates as well. At the same time, the dominant ATPase activity in many plasma membrane preparations was shown to be dis- tinct from the ion-pump ATPases, but had similar enzymatic properties as the ecto-AT- Pase(s). Thus the term "E-type ATPase activity" has been proposed for ATPase activity exhibiting these characteristics, and it is assumed that all ecto-ATPases are E-type AT- Pases. The converse is not true, however, since soluble E-type ATPases were shown to ex- sist in plants, microorganisms, and the saliva of blood sucking insects. These enzymes could be easily purified, and exhibited very high specific activity.