Amino terminal acetylation and the levels of some erythrocyte proteins
โ Scribed by N. Spencer; N. Carter
- Publisher
- Elsevier Science
- Year
- 1977
- Tongue
- English
- Weight
- 526 KB
- Volume
- 67
- Category
- Article
- ISSN
- 0022-5193
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
The amino acid sequence of the high-activity equine erythrocyte carbonic anhydrase (CA-II) has been determined. Two different N-termini are noted, the C1 form having an N-acetyl-serine and the C2 form an N-acetyl-threonine. The sequence of the equine enzyme is most homologous to the human CA-II isoz
Erythropoietin (EP) controls the terminal phase of differentiation in which proerythroblasts and their precursors, the colony forming units-erythroid (CFU-e), develop into erythrocytes. Biochemical studies of this hormonedirected terminal differentiation have been hindered by t h e lack of a homogen
The metabolic generation of N2-acetylphenelzine by rats treated with phenelzine, and the activity of this metabolite as an inhibitor of monoamine oxidase enzymes in vivo were confirmed. The isomeric amide N1-acetylphenelzine was not a metabolic product of phenelzine and also did not inhibit monoamin