Derepressed leucine transport activity inEscherichia coli
โ Scribed by Rahmanian, Mohamad ;Oxender, Dale L.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1972
- Tongue
- English
- Weight
- 215 KB
- Volume
- 1
- Category
- Article
- ISSN
- 0091-7419
No coin nor oath required. For personal study only.
โฆ Synopsis
& are c o o r d i n a t e l y cont r o l l e d by t h e l e v e l of l e u c i n e i n t h e growth medium. Spontaneous mutants (Q) which c a n u t i l i z e D-leucine as a s o u r c e of L-leucine show d e r e p r e s s e d t r a n s p o r t a c t i v i t y f o r t h e three-branched c h a i n amino a c i d s .
๐ SIMILAR VOLUMES
A LD-carboxypeptidase from Escherichia coli K 12 was isolated by Tris-EDTA treatment and purified to electrophoretic homogeneity by DEAE-cellulose chromatography. The enzyme has a molecular weight of approximately 12,000 as determined by sodium dodecyl sulfatepolyacrylamide electrophoresis and by Se