Abstract：
:The gene for human pancreatic cholesterol esterase consists of 11 exons and 10 introns and is 9.2 kb in length. The last and longest exon (841 nucleotides) is unique to the human gene. Functional amino acids are encoded on separate exons. The leader sequence is encoded by a single exon which carries two additional N-terminal amino acids of the mature functional protein. A positive TATA element is identified 43 nucleotides from the start codon. Pulse-field gel electrophoresis and hybridization with various cDNA probes and direct sequence data revealed the existence of a CEase-like gene. Partial sequence analysis of this gene from a human cosmid library and human genomic DNA showed a premature stop signal in exon 10, shortly after the codon for the active-site histidine. Both the functional gene and the CEase-like gene have a polyadenylation signal in the 3'-untranslated region. Thus, the complex gene structure for this intestinally active enzyme may provide in part a potential molecular explanation for the well-known heterogeneity of the intestinal absorption of cholesterol.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Kumar BV,Aleman-Gomez JA,Colwell N,Lopez-Candales A,Bosner MS,Spilburg CA,Lowe M,Lange LGdoi
10.1021/bi00141a017subject
Has Abstractpub_date
1992-07-07 00:00:00pages
6077-81issue
26eissn
0006-2960issn
1520-4995journal_volume
31pub_type
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