MOLECULAR CONFORMATION OF EGG-WHITE LYSOZYME AND BOVINE ALPHA-LACTALBUMIN IN SOLUTION
MOLECULAR CONFORMATION OF EGG-WHITE LYSOZYME AND BOVINE ALPHA-LACTALBUMIN IN SOLUTION
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DOI：
10.1021/bi00807a024
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发表时间：
1970-01-01
期刊：
影响因子：
2.9
通讯作者：
KUGLER, FR
中科院分区：
文献类型：
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作者：
KRIGBAUM, WR;KUGLER, FR
WR Krigbaum 和 FR Kügler 摘要：报道了鸡蛋清溶菌酶和牛乳清蛋白的小角衍射测量结果。这两种酶的氨基酸序列表现出相当大的同源性，这表明它们可能具有相似的三级结构。溶菌酶的回转半径 R 为 14.3 A，其等效散射体为长椭球体，尺寸为 28 X 28 X 50 A，而乳清蛋白的 R= 16.7 A，其等效椭球体为扁椭球体，尺寸为 22 X 44 X 57 A。因此，我们得出结论，溶菌酶和乳清蛋白具有 I-/ysozymes 形式一个 在脊椎动物的许多器官、组织和分泌物以及细菌、噬菌体和植物中发现的一类广泛分布的酶。此类成员的分子量可能有很大差异，但都表现出通过胞壁酶的作用快速裂解细菌细胞壁的共同能力。对 T4 噬菌体溶菌酶（Tsugita 和 Inoye，1968）和鸡蛋清溶菌酶（Jollés 等，1963；Canfield，1963）的氨基酸序列进行比较，发现没有共同的一级结构，尽管在碱性、酸性和疏水侧链的相对数量方面存在一些组成相似性。下面我们将鸡蛋清溶菌酶简称为溶菌酶。
WR Krigbaum and FR Kügler abstract: Small angle diffraction measurements are reported for hens egg-white lysozyme andbovine-lactalbumin. The amino acid sequences of these two enzymes exhibit con-siderable homology, which has ledto the suggestion that they may have similartertiary structures. Lysozyme has a radius of gyration, R, of 14.3 A, and its equivalent scattering body is a prolate ellipsoid having dimensions 28 X 28 X 50 A, while-lactalbumin has R= 16.7 A, and its equivalent ellipsoid is oblate with'dimensions 22 X 44 X 57 A. We therefore conclude that lysozyme and-lactalbumin haveI—/ysozymes form a class of widely distributed enzymes found in a number of organs, tissues, and secretions of vertebrates, as well as in bacteria, phages, and plants. Members of this class may differ considerably in molecular weight, but all exhibit a common capability to rapidly lyse bacterial cell walls by their action as muramidases. Comparison of the amino acid sequence of T4phage lysozyme (Tsugita and Inoye, 1968) and hens egg-white lysozyme (Jollés et al., 1963; Canfield, 1963) revealed no common primary structure, although there was some compositional similarity in terms of the relative numbers of basic, acidic, and hydrophobic side chains. In the following we shall refer to hens egg-white lysozyme as lysozyme.