Godovac-Zimmermann J, Sheil M, Wrench P M, Hiller R G
John Curtin School of Medical Research, Australian National University, Canberra, ACT.
Biochim Biophys Acta. 1992 Mar 27;1120(1):117-21. doi: 10.1016/0167-4838(92)90432-d.
The full amino acid sequence of the beta-subunit of Chroomonas CS24 phycoerythrin has been determined by conventional Edman degradation and mass spectrometry. The sequence compromises 177 amino acids with a molecular mass of 18669 Da. It is 91.5% identical to the deduced amino acid sequence of Cryptomonas phi beta-phycoerythrin (Reith, M. and Douglas, S. (1990) Plant Mol. Biology 15, 585-592). The chromophores are bound by single thioether linkages. No evidence of microheterogeneity was found confirming that both beta-subunits of the holoprotein are identical.
通过传统的埃德曼降解法和质谱分析法,已确定了嗜色藻CS24藻红蛋白β亚基的完整氨基酸序列。该序列由177个氨基酸组成,分子量为18669道尔顿。它与隐藻属phiβ-藻红蛋白推导的氨基酸序列有91.5%的同源性(Reith, M.和Douglas, S.(1990年)《植物分子生物学》15卷,585 - 592页)。发色团通过单一硫醚键相连。未发现微异质性的证据,证实全蛋白的两个β亚基是相同的。