HYDROXYARGININE-CONTAINING POLYPHENOLIC PROTEINS IN THE ADHESIVE PLAQUES OF THE MARINE MUSSEL MYTILUS-EDULIS
HYDROXYARGININE-CONTAINING POLYPHENOLIC PROTEINS IN THE ADHESIVE PLAQUES OF THE MARINE MUSSEL MYTILUS-EDULIS
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DOI：
10.1074/jbc.270.34.20183
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发表时间：
1995-08-25
影响因子：
4.8
通讯作者：
WAITE, JH
中科院分区：
文献类型：
--
作者：
PAPOV, VV;DIAMOND, TV;WAITE, JH
从海洋贻贝贻贝的足底粘附斑和足中分离出一种不寻常的多态性蛋白家族，该家族包含九个或更多变体。按照既定的术语，该家族被称为IM。 edulis 脚蛋白 3 或简称为 Mefp-3。 Mefp-S 的变体的分子量约为 6 kDa，等电点大于 10.5，氨基酸组成以六种氨基酸为主：甘氨酸、天冬酰胺、3,4-二羟基苯丙氨酸（多巴）、色氨酸、精氨酸和未知的碱性氨基酸。后者已使用快原子轰击质谱法和适当的标准品分离并鉴定为 4-羟基精氨酸。变体 Mefp-3F 的一级结构已通过肽图谱确定，使用自动 Edman 测序结合快原子轰击和基质辅助激光解吸电离质谱法：ADYYGPNYGPPRRYGGGNYNRYNRYGRRYGGYKGWNNGWNRGRRGKYW，其中 Y 代表 Dopa，R 代表 羟基精氨酸。值得注意的是，RY 的 4 次出现都以对胰蛋白酶消化的抵抗为标志。尽管酪氨酸基本完全转化为多巴，但精氨酸的羟基化程度在 40% 至 80% 之间。与其他贻贝粘附蛋白（例如 Mefp-1 和 -2）具有大量高度保守、串联重复的肽基序相比，Mefp-3 仅具有短的零星重复序列。 Mefp-3 在足足粘连中的具体功能尚不清楚。
An unusual polymorphic protein family of nine or more variants has been isolated from the byssal adhesive plaques and foot of the marine mussel Mytilus edulis. In accordance with established terminology, the family is referred to as IM. edulis foot protein 3 or simply Mefp-3. Variants of Mefp-S have molecular masses of about 6 kDa, isoelectric points greater than 10.5, and an amino acid composition dominated by six amino acids: glycine, asparagine, 3,4-dihydroxyphenylalanine (Dopa), tryptophan, arginine, and an unknown basic amino acid. The latter has been isolated and identified as 4-hydroxyarginine using fast atom bombardment mass spectrometry and appropriate standards. The primary structure of variant Mefp-3F has been determined by peptide mapping using automated Edman sequencing in combination with fast atom bombardment and matrix-assisted laser desorption ionization mass spectrometry: ADYYGPNYGPPRRYGGGNYNRYNRYGRRYGGYKGWNNGWNRGRRGKYW where Y represents Dopa, and R represents hydroxyarginine. Notably, the 4 occurrences of RY are marked by a resistance to trypsin digestion. Although the conversion of tyrosines to Dopa is essentially complete, hydroxylation of arginines varies between 40 and 80%. In contrast to other mussel adhesive proteins such as Mefp-1 and -2 which have large numbers of highly conserved, tandemly repeated peptide motifs, Mefp-3 has only short sporadic repeats. The specific function of Mefp-3 in byssal adhesion is unknown.