Biosynthesis of hypusine in eIF-4D precursors.

作者: M. H. Park , E. C. Wolff , A. Abbruzzese , J. E. Folk

DOI: 10.1007/978-1-4684-5637-0_38

关键词:

摘要: An unusual basic amino acid hypusine was discovered in 1971 extracts of bovine brain by Shiba and coworkers, who determined its chemical structure as Ne -(4-amino-2-hydroxybutyl)lysine(1). Its distribution various animal tissues the free (2) a component protein (3) subsequently reported. Initial attempts to isolate any specific that contained were unsucessful, however (3). Ten years after discovery hypusine, we observed radiolabeling single cellular (Mr 183000, pI 5.3) upon incubation human peripheral lymphocytes with [1, 8- 3H] spermidine or [2, 3- putrescine presence mitogen, phytohemagglutinin identified polyamine-derived radioactive this (4).

参考文章(26)
R J Murphey, E W Gerner, Hypusine formation in protein by a two-step process in cell lysates. Journal of Biological Chemistry. ,vol. 262, pp. 15033- 15036 ,(1987) , 10.1016/S0021-9258(18)48133-1
M H Park, T Y Liu, S H Neece, W J Swiggard, Eukaryotic initiation factor 4D. Purification from human red blood cells and the sequence of amino acids around its single hypusine residue. Journal of Biological Chemistry. ,vol. 261, pp. 14515- 14519 ,(1986) , 10.1016/S0021-9258(18)66899-1
Kari I. Kivirikko, Raili Myllylä, Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes. Methods in Enzymology. ,vol. 82, pp. 245- 304 ,(1982) , 10.1016/0076-6879(82)82067-3