✦ LIBER ✦

Enhancement of photophosphorylation and photoreduction by a chloroplast factor from spinach leaves

✍ Scribed by Robert Gee; Anders Kylin; Paul Saltman

Book ID: 118852182
Publisher: Elsevier Science
Year: 1970
Tongue: English
Weight: 290 KB
Volume: 40
Category: Article
ISSN: 0006-291X
DOI: 10.1016/0006-291x(70)90952-6

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Purification and Characterization of Chl

Purification and Characterization of Chloroplast Dehydroascorbate Reductase from Spinach Leaves

✍ Shimaoka, T.; Yokota, A.; Miyake, C. 📂 Article 📅 2000 🏛 Oxford University Press 🌐 English ⚖ 535 KB

Separation and Partial Characterization

Separation and Partial Characterization of Chloroplast and Non-chloroplast a-Glucan Phosphorylases from Spinach Leaves

✍ Steup, Martin; Schachtele, Christoph; Latzko, Erwin 📂 Article 📅 1980 🏛 Elsevier ⚖ 555 KB

Current Protocols in Cell Biology || Pur

Current Protocols in Cell Biology || Purification of Intact Chloroplasts from Arabidopsis and Spinach Leaves by Isopycnic Centrifugation

✍ Bonifacino, Juan S.; Dasso, Mary; Harford, Joe B.; Lippincott-Schwartz, Jennifer 📂 Article 📅 2008 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 212 KB

Enhancement of emission from chloroplast

Enhancement of emission from chloroplasts at 698 nm by a naturally-occurring factor

✍ M. Brody; B. Nathanson; W.S. Cohen 📂 Article 📅 1969 🏛 Elsevier Science 🌐 English ⚖ 175 KB

Some observations on biosynthesis and ra

Some observations on biosynthesis and ratio regulation of mono- and digalactosyl diglycerides by chloroplasts and other subcellular fractions from spinach leaves

✍ van Hummel, Hans C. 📂 Article 📅 1974 🏛 Elsevier ⚖ 770 KB

Properties and physiological function of

Properties and physiological function of a glutathione reductase purified from spinach leaves by affinity chromatography

✍ B. Halliwell; C. H. Foyer 📂 Article 📅 1978 🏛 Springer-Verlag 🌐 English ⚖ 862 KB

Glutathione reductase (EC 1.6.4.2) was purified from spinach (Spinacia oleracea L.) leaves by affinity chromatography on ADP-Sepharose. The purified enzyme has a specific activity of 246 enzyme units/mg protein and is homogeneous by the criterion of polyacrylamide gel electrophoresis on native and S