Jauregui-Adell J, Pechere J F
Biochim Biophys Acta. 1978 Sep 26;536(1):263-8. doi: 10.1016/0005-2795(78)90072-7.
Parvalbumins from coelacanth (Latimeria chalumnae) myogen have been isolated by gel filtration of Sephadex G-75 and DEAE-cellulose chromatography. Disc electrophoresis and cellulose acetate electrophoresis showed the homogeneity of the three first major parvalbumin peaks (pI = 5.44, pI = 4.95 and pI = 4.52). The fourth component was partially resolved into two more parvalbumins (pI = 3.78 and pI = 3.50) by preparative gel electrophoresis. Amino acid analyses and tryptic peptide maps separated the five components in two major categories. The two less acidic components differ only in the presence or absence of an N-terminal blocking group. The three more acidic components constitute the second category; in spite of this heterogeneity, they share the same amino acid sequence.
通过Sephadex G - 75凝胶过滤和DEAE - 纤维素色谱法从腔棘鱼（Latimeria chalumnae）肌原蛋白中分离出了小白蛋白。圆盘电泳和醋酸纤维素电泳显示了前三个主要小白蛋白峰（pI = 5.44、pI = 4.95和pI = 4.52）的同质性。通过制备性凝胶电泳，第四个组分部分分离为另外两种小白蛋白（pI = 3.78和pI = 3.50）。氨基酸分析和胰蛋白酶肽图将这五个组分分为两大类。两种酸性较弱的组分仅在是否存在N端封闭基团上有所不同。三种酸性较强的组分构成第二类；尽管存在这种异质性，但它们具有相同的氨基酸序列。
