Goustin A S, Wilt F H
Biochim Biophys Acta. 1982 Oct 29;699(1):22-7. doi: 10.1016/0167-4781(82)90167-1.
Regulation of protein synthesis can be exercised at a number of levels. One of the more experimentally difficult levels to approach has been the measurement of peptide elongation rate. This paper presents a new application of the cyanogen bromide (CNBr) cleavage of proteins in a direct measurement of histone peptide elongation rate in cleaving sea urchin embryos (Strongylocentrotus purpuratus). The data indicate an elongation rate (at 15 degrees C) for histones H2B and H1 alpha of 0.69 and 0.80 codons per s, respectively. These values fall within the range of previously published values of average peptide elongation rate for total protein in these cells. This method should be generally applicable to many systems for which the measurement of peptide elongation rate may provide a key to the understanding of the regulation of protein synthesis.
蛋白质合成的调控可以在多个层面上进行。在实验上较难研究的层面之一是肽链延伸速率的测量。本文介绍了溴化氰（CNBr）裂解蛋白质在直接测量分裂海胆胚胎（紫海胆）中组蛋白肽链延伸速率方面的新应用。数据表明，在15℃时，组蛋白H2B和H1α的延伸速率分别为每秒0.69和0.80个密码子。这些值落在先前发表的这些细胞中总蛋白质平均肽链延伸速率值的范围内。这种方法应该普遍适用于许多系统，对于这些系统而言，肽链延伸速率的测量可能是理解蛋白质合成调控的关键。
