✦ LIBER ✦

An insoluble complex formed by the interaction of muscle phosphorylase with glycogen

✍ Scribed by Zvi Selinger; Michael Schramm

Book ID: 118848256
Publisher: Elsevier Science
Year: 1963
Tongue: English
Weight: 346 KB
Volume: 12
Category: Article
ISSN: 0006-291X
DOI: 10.1016/0006-291x(63)90191-8

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

The interaction of muscle glycogen phosp

The interaction of muscle glycogen phosphorylase b with glycogen

✍ S.V. Klinov; N.A. Chebotareva; N.P. Lissovskaya; D.R. Davidov; B.I. Kurganov 📂 Article 📅 1982 🏛 Elsevier Science 🌐 English ⚖ 564 KB

Studies on interaction of phosphorylase

Studies on interaction of phosphorylase kinase from rabbit skeletal muscle with glycogen in the presence of ATP and ADP

✍ Iraida E. Andreeva; Valentina F. Makeeva; Nataliya B. Livanova; Sergey P. Petukh 📂 Article 📅 2001 🏛 Elsevier Science 🌐 English ⚖ 288 KB

The complete tetramerization of rabbit m

The complete tetramerization of rabbit muscle glycogen phosphorylase b by AMP and salt. An analytical ultracentrifuge study

✍ Sáid A. Assaf; Adel A. Yunis 📂 Article 📅 1971 🏛 Elsevier Science 🌐 English ⚖ 896 KB

The selective adsorption of rabbit-muscl

The selective adsorption of rabbit-muscle glycogen phosphorylase by potato starch a two-step procedure for isolation of the enzyme in pure form

✍ G. De La Haba 📂 Article 📅 1962 🏛 Elsevier Science ⚖ 737 KB

Properties of the complexes formed by 1-

Properties of the complexes formed by 1-anilinonaphthalene-8-sulfonate with phosphorylase kinase and calmodulin

✍ R. F. Steiner; H. Sternberg 📂 Article 📅 1982 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 710 KB

## Abstract Phosphorylase kinase contains four approximately equivalent binding sites for 1‐anilinonaphthalene‐8‐sulfonate (1,8‐ANS). Measurements of the time decay of fluorescence anisotropy have failed to give any indication of internal degrees of rotational freedom involving a significant portio

The hepatic PP1 glycogen-targeting subun

The hepatic PP1 glycogen-targeting subunit interaction with phosphorylase a can be blocked by C-terminal tyrosine deletion or an indole drug

✍ Ian R. Kelsall; Shonagh Munro; Irene Hallyburton; Judith L. Treadway; Patricia T 📂 Article 📅 2007 🏛 Elsevier Science 🌐 English ⚖ 347 KB