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- W2477909765 abstract "This chapter examines the factors that influence the N α -acetylation of ACTH and fragments of ACTH. The rat pituitary contains an enzyme that acetylates the α-amino group of the NH 2 -terminal serine residue of corticotropin (ACTH) and the structurally related peptide, des-N α -acetyl α-melanotropin, using acetyl CoA. The enzyme works equally well with ACTH (1–39) , ACTH (1–24) , and ACTH (1–10) , but will not utilize Ser or Ser.Tyr, suggesting that the information required for N α -acetylation by the enzyme resides in the first 10 amino acids. The product of the acetylation of des-acetyl α-melanotropin was shown to be identical to α-melanotropin (α-MSH). Removal of the NH 2 -terminal serine residue of des-N α -acetyl α-MSH by Edman degradation results in the formation of a peptide which is no longer a substrate for the enzyme. The reaction of the enzyme with ACTH (1–10) is also specific for the α-amino group of the NH 2 -terminal amino acid as determined by identification of N-[ 3 H] acetyl serine. The N α -acetyltransferase is localized predominantly in the subcellular fractions sedimenting at forces greater than 10,000×g." @default.
- W2477909765 created "2016-08-23" @default.
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- W2477909765 date "1979-01-01" @default.
- W2477909765 modified "2023-09-27" @default.
- W2477909765 title "FACTORS WHICH INFLUENCE THE Nα-ACETYLATION OF ACTH AND FRAGMENTS OF ACTH Supported by USPHS Grant #AM 18024." @default.
- W2477909765 doi "https://doi.org/10.1016/b978-0-12-604450-8.50052-3" @default.
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