The amino-acid sequence and carbohydrate content of phospholipase A2 from bee venom.
The amino-acid sequence and carbohydrate content of phospholipase A2 from bee venom.
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蜂毒磷脂酶 A2 的氨基酸序列和碳水化合物含量。
DOI：
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发表时间：
1974
期刊：
影响因子：
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通讯作者：
C. A. Vernon
中科院分区：
文献类型：
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作者：
R. Shipolini;G. L. Callewaert;R. Cottrell;C. A. Vernon
测定了欧洲蜜蜂（Apis mellifica）毒液中磷脂酶A2的完整氨基酸序列。n端氨基酸残基序列通过直接应用Edman降解技术得到，c端氨基酸残基序列通过羧肽酶A和b酶切得到。还原酶和羧甲基化酶与胰蛋白酶酶切得到完全可溶的肽混合物，分离出所有成分并确定其结构。通过胰凝乳蛋白酶消化还原酶和羧甲基化酶以及裂解赖氨酸残基的蛋白酶消化还原酶和氨基乙化酶分离出的肽的结构，可以推断出胰蛋白酶的重叠部分。剩下的两个歧义是通过从胰蛋白酶的还原、羧甲基化和马来酰化酶的消化得到的肽来解决的。磷脂酶A2由一条由128个氨基酸残基组成的单链组成，并含有附着的碳水化合物残基。确定了碳水化合物部分的组成和附着点。
The complete amino acid sequence of phospholipase A2 from the venom of the common European honey-bee (Apis mellifica) has been determined. The sequence of amino acid residues at the N-terminus was obtained by direct application of the Edman degradation technique and that at the C-terminus by digestion with carboxypeptidases A and B. Digestion of the reduced and carboxymethylated enzyme with trypsin yielded a completely soluble peptide mixture, all the components of which were isolated and their structures determined. Overlaps of the tryptic peptides were deduced from the structures of peptides isolated after digestion of the reduced and carboxymethylated enzyme with chymotrypsin and of the reduced and aminoethylated enzyme with a protease specific for cleavage at lysine residues. Two remaining ambiguities were resolved by peptides obtained from a digest of the reduced, carboxymethylated and maleylated enzyme with trypsin. The phospholipase A2 consists of a single chain of 128 amino acid residues and contains attached carbohydrate residues. The composition and point of attachment of the carbohydrate moiety have been established.