Structural Studies of Human Plasma Membrane Anion Exchanger, AE1, Expressed in Saccharomyces cerevisiae
                    
                        
                            نویسندگان
                            
                            
                        
                        
                    
                    
                    چکیده
منابع مشابه
Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop. Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained ...
متن کاملCLONING AND EXPRESSION OF HUMAN IFNα2B GENE IN SACCHAROMYCES CEREVISIAE
Interferon is a protein secreted by eucaryotic cells following stimulation by viruses, bacteria, and many other immunogenes. Recent medical studies indicate that interferons have effective role in the treatment of virus infections, immunodeficiency and certain types of cancer such as hairy cell leukaemia (HCL). The aim of the present study is to apply yeast strain for secreting human IFNα2b fol...
متن کاملStructural model for the organization of the transmembrane spans of the human red-cell anion exchanger (band 3; AE1).
We have examined the functional co-assembly of non-complementary pairs of N- and C-terminal polypeptide fragments of the anion transport domain (b3mem) of human red-cell band 3. cDNA clones encoding non-contiguous pairs of fragments with one transmembrane (TM) region omitted, or overlapping pairs of fragments with between one and ten TM regions duplicated, were co-expressed in Xenopus oocytes a...
متن کاملTopology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642. We have shown that the integrity of six different loops are not essential for stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes. We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and...
متن کاملThe structure of the human red blood cell anion exchanger (EPB3, AE1, band 3) gene.
The structure and sequence of the human red blood cell anion exchanger (EPB3, AE1, band 3) gene was determined by analysis of genomic and cDNA clones. The gene extends over 18 kb and consists of 20 exons. The cDNA sequence comprises 4,906 nucleotides [excluding the poly(A) tail]. There is extensive similarity between the human and mouse AE1 gene, although the latter covers 17 kb. The additional...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2009
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.23.1_supplement.800.5