Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase
作者： A E Pegg , N B Applegren , S J Ervin , R A Casero , P Celano
DOI: 10.1016/S0021-9258(17)35245-6
关键词: cDNA library 、 Polyamine Analogue 、 Spermidine 、 Polyamine 、 Spermine 、 Biochemistry 、 Molecular biology 、 Acetyltransferase 、 Peptide sequence 、 Complementary DNA 、 Biology
摘要: Spermidine/spermine N1-acetyltransferase (Spd/Spm acetyltransferase) is the rate-limiting enzyme in catabolism of polyamines. This highly inducible by several stimuli, including natural polyamines and their structural analogues. To investigate underlying mechanism responsible for control this a cDNA which codes an active human Spd/Spm acetyltransferase has been isolated from random primed library constructed mRNA polyamine analogue treated large cell lung carcinoma line, NCI H157. The 972-base pair was identified using 32-fold degenerate, 20-base oligomer probe to 7-amino acid polypeptide sequence derived purified protein. 513-base open reading frame that protein 171 amino acids with predicted molecular weight 20,023. In vitro translation studies demonstrated product be biologically enzyme. recognizes 1.5-kilobase transcript cells induced H157 line following treatment analogue. unusually high expression response does not appear result amplification gene.
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