✦ LIBER ✦

Photoaffinity labelling of lactate dehydrogenase from pig heart with a bifunctional NAD+-analogue

✍ Scribed by Susanne Becker; Tomas Bergman; Lars Hjelmqvist; Reinhard Jeck; Hans Jörnvall; Hanno Leibrock; Christoph Woenckhaus

Book ID: 113269770
Publisher: Elsevier Science
Year: 1996
Tongue: English
Weight: 550 KB
Volume: 1293
Category: Article
ISSN: 0167-4838
DOI: 10.1016/0167-4838(95)00268-5

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Synthesis of spin-labeled photoaffinity

Synthesis of spin-labeled photoaffinity derivatives of NAD+ and their interaction with lactate dehydrogenase

✍ A. Wolf; T.M. Fritzsche; B. Rudy; W.E. Trommer 📂 Article 📅 1987 🏛 Elsevier Science 🌐 English ⚖ 478 KB

Ternary complex formation of pig heart l

Ternary complex formation of pig heart lactate dehydrogenase with spin-labelled coenzymes and inhibitors as studied by electron spin resonance

✍ Herbert R. Wenzel; Wolfgang E. Trommer 📂 Article 📅 1979 🏛 Elsevier Science ⚖ 517 KB

Effects of GTP analogues and activation

Effects of GTP analogues and activation of endogenous protein kinases on photoaffinity labeling with [3H](+)PN200-110 of crude membranes from rat heart and brain

✍ Seiji Ichida; Atuhiro Masada; Takuya Yoshioka; Hiroyuki Kishino; Takafumi Akimot 📂 Article 📅 1992 🏛 Elsevier Science 🌐 English ⚖ 508 KB

Isolation and properties of glyceraldehy

Isolation and properties of glyceraldehyde-3-phosphate dehydrogenase from a sturgeon from the Caspian Sea and its interaction with spin-labeled NAD+ derivatives

✍ Matthias P. Deparade; Klaus Glöggler; Wolfgang E. Trommer 📂 Article 📅 1981 🏛 Elsevier Science ⚖ 731 KB

Ultracentrifugation studies of the locat

Ultracentrifugation studies of the location of the site involved in the interaction of pig heart lactate dehydrogenase with acidic phospholipids at low pH. A comparison with the muscle form of the enzyme

✍ Grzegorz Terlecki; Elżbieta Czapińska; Katarzyna Hotowy 📂 Article 📅 2007 🏛 SP Versita 🌐 English ⚖ 597 KB

## Abstract Lactate dehydrogenase (LDH) from the pig heart interacts with liposomes made of acidic phospholipids most effectively at low pH, close to the isoelectric point of the protein (pH = 5.5). This binding is not observed at neutral pH or high ionic strength. LDH-liposome complex formation re

Purification and properties of the heart

Purification and properties of the heart type lactate dehydrogenase of the cod (Gadus morhua) from the baltic sea: Comparison with LDH-A4 and LDH-C4

✍ Marek S. Ziȩtara; Edward F. Skorkowski 📂 Article 📅 1993 🏛 Elsevier Science 🌐 English ⚖ 743 KB