文章基本信息

标题：Sorting-out of acceptor-donor relationships in the transglutaminase-catalyzed cross-linking of crystallins by the enzyme-directed labeling of potential sites
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作者：L Lorand ; K N Parameswaran ; P T Velasco 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1991
卷号：88
期号：1
页码：82-83
DOI：10.1073/pnas.88.1.82
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The dansyl-conjugated (Dns) peptides Dns-Pro-Gly-Gly-Gln-Gln-Ile-Val and Dns-Ala-Gln-Gln-Ile-Val, patterned on the N-terminal sequence of fibronectin, were synthesized and used for the transglutaminase (protein-glutamine:amine gamma-glutamyltransferase, EC 2.3.2.13 )-directed selective blocking of lens proteins that otherwise might participate in donating lysyl side chains in forming N epsilon-(gamma-glutamyl)-lysine cross-linked oligomers and polymers. Labeling profiles with these peptides could be readily visualized by fluorescence as well as by immunoblotting with anti-dansyl antibody. The labeling patterns in rabbit lens homogenates were quite different with the dansylated peptides than those obtained with dansylcadaverine. Use of such glutamine-containing dansylated peptides should clearly aid in identifying, isolating, and sequencing potential donor substrates of transglutaminases in many biological systems.