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Studies onthe chemical nature of lysine-binding sites and on their localization in human plasminogen.

作者信息

Lerch P G, Rickli E E

出版信息

Biochim Biophys Acta. 1980 Oct 21;625(2):374-8. doi: 10.1016/0005-2795(80)90302-5.

DOI:10.1016/0005-2795(80)90302-5
PMID:6776996
Abstract

The isolated 'kringle' structures 1 and 4 of human plasminogen lost lysine affinity upon photo-oxidation of histidine, but mostly retained it in the presence of 6-aminohexanoic acid. Lysine affinity was lost and could be partially restored after blocking of histidine with diethylpyrocarbonate and deblocking, or after esterification of COOH-groups and saponification. Only His-31 and most likely Asp-54 qualify as participants in a lysine binding site when the primary structures of the 'kringles' are considered.

摘要

相似文献

1
Studies onthe chemical nature of lysine-binding sites and on their localization in human plasminogen.
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2
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J Biol Chem. 1981 Nov 10;256(21):11172-6.

引用本文的文献

1
Structural/functional properties of the Glu1-HSer57 N-terminal fragment of human plasminogen: conformational characterization and interaction with kringle domains.人纤溶酶原Glu1-HSer57 N端片段的结构/功能特性：构象表征及与kringle结构域的相互作用
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2
Partial amino acid sequence of apolipoprotein(a) shows that it is homologous to plasminogen.载脂蛋白(a)的部分氨基酸序列表明它与纤溶酶原同源。
Proc Natl Acad Sci U S A. 1987 May;84(10):3224-8. doi: 10.1073/pnas.84.10.3224.