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
โฆ LIBER โฆ
ld-Carboxypeptidase activity inEscherichia coli
โ Scribed by Renate Metz; Susanne Henning; Walter P. Hammes
- Publisher
- Springer
- Year
- 1986
- Tongue
- English
- Weight
- 624 KB
- Volume
- 144
- Category
- Article
- ISSN
- 0302-8933
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