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Cloning and characterization of a cDNA for rat tissue-type plasminogen activator.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
1988 (English)In: DNA (Mary Ann Liebert, Inc.), ISSN 0198-0238, Vol. 7, no 10, 671-7 p.Article in journal (Refereed) Published
Abstract [en]

Two partly overlapping lambda gt11 cDNA clones coding for the 22S rat tissue-type plasminogen activator (t-PA) mRNA were isolated. The cDNA sequences cover 2445 nucleotides of the mRNA, including a 5' untranslated region of 31 nucleotides, an open reading frame of 1677 nucleotides, a 3' untranslated region of 737 nucleotides, and a poly(A) tail. The open reading frame codes for a 17-amino-acid signal peptide, a propeptide with 12 amino acids, and the mature protein with 530 amino acids. Rat t-PA has 81% and 92% amino acid sequence identity with the human and mouse counterparts and an equal distribution of conserved amino acids, suggesting that the proteins can fold into identical three-dimensional structures. The rat t-PA sequence contains two putative N-glycosylation sites at Asn-120 and Asn-452, while human t-PA has an additional glycosylation site at Asn-187. The site at Asn-187 is glycosylated in the human protein, revealing a different glycosylation pattern between the human and rat proteins.

Place, publisher, year, edition, pages
1988. Vol. 7, no 10, 671-7 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:umu:diva-59886PubMedID: 3148445OAI: diva2:556987
Available from: 2012-09-26 Created: 2012-09-26 Last updated: 2012-09-26

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