Buckley D I, Houghten R A, Ramachandran J
Int J Pept Protein Res. 1981 Apr;17(4):508-13. doi: 10.1111/j.1399-3011.1981.tb02021.x.
In the course of isolation of alpha-melanotropin (alpha-MSH) from porcine pituitary extracts, a peptide with identical amino acid composition but slightly less polar properties compared to alpha-MSH was detected and isolated by partition chromatography. The new peptide was identified as N, O-diacetyl-Ser1-alpha-MSH by high resolution nuclear magnetic resonance spectroscopy. N, O-diacetyl-Ser1-alpha-MSH was readily converted to alpha-MSH by incubation at pH 9.5. The O-acetyl analog of alpha-MSH was found to be as active as alpha-MSH in stimulating lipolysis in isolated rabbit adipocytes.
在从猪垂体提取物中分离α-促黑素(α-MSH)的过程中,通过分配色谱法检测并分离出一种与α-MSH氨基酸组成相同但极性略小的肽。通过高分辨率核磁共振光谱法将这种新肽鉴定为N,O-二乙酰基-Ser1-α-MSH。N,O-二乙酰基-Ser1-α-MSH在pH 9.5下孵育可轻易转化为α-MSH。发现α-MSH的O-乙酰基类似物在刺激离体兔脂肪细胞的脂肪分解方面与α-MSH具有相同的活性。