Abstract
The nucleotide and complete amino acid sequence for the human ß2-glycoprotein I (ß,I) was derived by sequencing the cDNA clone pB2I- 1. In addition to the 326 amino acid residues of the mature protein this clone codes for a putative leader peptide and contains sequence representing 5' and 3' untranslated regions. When this amino acid sequence was compared with the previously published primary sequence, three major amino acid substitutions were found, two involving cysteine residues. These substitutions lead to a new alignment of the complement control protein (CCP) repeats present in fl2I and a prediction of the complete disulphide bond organization. Northern-blot analysis indicates that hepatocytes are a major site of biosynthesis for this protein. A transcription signal of about 1.5 kb was detected by using RNA from HepG2 cells
Item Type: | Journal article |
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Faculties: | Biology |
Subjects: | 500 Science > 570 Life sciences; biology |
URN: | urn:nbn:de:bvb:19-epub-3046-1 |
Language: | English |
Item ID: | 3046 |
Date Deposited: | 07. Apr 2008, 12:07 |
Last Modified: | 04. Nov 2020, 12:46 |