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鸡卵清溶菌酶中103位残基的鉴定。

Identification of residue 103 in hen egg-white lysozyme.

作者信息

Imoto T, Okazaki K, Yamada H, Fujita K, Yamato T, Koga D

出版信息

J Biochem. 1981 Oct;90(4):991-5. doi: 10.1093/oxfordjournals.jbchem.a133585.

Abstract

Since it has been uncertain whether residue 103 in hen egg-white lysozyme is aspartic acid or asparagine, we reexamined the identity of this residue. To avoid complication, the tryptic peptide T-13 (Ile 98-Arg 112) was further cleaved. The peptide containing residues Gly 102-Arg 112 was obtained by tryptic digestion of lysozyme modified at Asp 101 with diethylenetriamine. The peptide containing residues Ile 98-homoserine 105 was obtained by BrCN treatment of peptide T-13. Both Edman degradation of the former peptide and carboxypeptidase X digestion of the latter peptide identified residue 103 in hen egg-white lysozyme as asparagine.

摘要

由于尚不确定鸡蛋清溶菌酶中的103位残基是天冬氨酸还是天冬酰胺,我们重新检查了该残基的身份。为避免复杂性,对胰蛋白酶肽T-13(Ile 98-Arg 112)进行了进一步切割。通过用二亚乙基三胺对101位天冬氨酸修饰的溶菌酶进行胰蛋白酶消化,得到了含有残基Gly 102-Arg 112的肽。通过用溴化氰处理肽T-13,得到了含有残基Ile 98-高丝氨酸105的肽。对前一种肽进行的埃德曼降解和对后一种肽进行的羧肽酶X消化均确定鸡蛋清溶菌酶中的103位残基为天冬酰胺。

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