𝔖 Bobbio Scriptorium
✦   LIBER   ✦

The involvement of aspartate aminotransferases in ammonium assimilation in lupin nodules

✍ Scribed by Paul H.S. Reynolds; Kevin J.F. Farnden

Publisher
Elsevier Science
Year
1979
Tongue
English
Weight
532 KB
Volume
18
Category
Article
ISSN
0031-9422

No coin nor oath required. For personal study only.

πŸ“œ SIMILAR VOLUMES

Carnosine prevents the glycation-induced
Carnosine prevents the glycation-induced changes in electrophoretic mobility of aspartate aminotransferase
✍ Norbert W. Seidler πŸ“‚ Article πŸ“… 2000 πŸ› John Wiley and Sons 🌐 English βš– 122 KB πŸ‘ 1 views

Carbohydrate-derived aldehydes cause irreversible loss of protein function via glycation. We previously observed that glyceraldehyde 3-phosphate (Glyc3P) abolishes the enzyme activity of cardiac aspartate aminotransferase (cAAT). We also examined the protective effects of carnosine against Glyc3P-in

Optimal conditions for protease use in t
Optimal conditions for protease use in the assay of serum mitochondrial aspartate aminotransferase
✍ Hiroaki Okabe; Yoshinori Uji; Hiroyuki Sugiuchi; Yoshifumi Watazu; Yasushi Shira πŸ“‚ Article πŸ“… 1990 πŸ› John Wiley and Sons 🌐 English βš– 331 KB

The optimal conditions for selective proteolytic inactivation of cytosolic aspartate aminotransferase (c-AST) to determine mitochondrial aspartate aminotransferase (m-AST) in serum were studied. Protease 401 was found to be effective over a pH range of 6.0-10.0. A pH of 9.5 with 0.5% albumin in the