| 1. |
- López Otin, C, et al.
(författare)
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The complete amino acid sequence of human complex-forming glycoprotein heterogeneous in charge (protein HC) from one individual
- 1984
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Ingår i: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861. ; 228:2, s. 54-544
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Tidskriftsartikel (refereegranskat)abstract
- The complete amino acid sequence of the single polypeptide chain of human complex-forming glycoprotein heterogeneous in charge (protein HC) isolated from a single individual is reported with the supporting data. The primary structure was determined by automatic degradation of the intact chain and of fragments obtained by chemical and enzymatic degradations of the native or reduced and S-carboxymethylated protein. The polypeptide chain of protein HC contained 182 amino acid residues with a calculated molecular weight of 20,621. No amino acid sequence variability was found and such variability can therefore not explain the great charge heterogeneity of protein HC in a single individual. The amino acid sequence of protein HC was nearly identical to the one reported for human alpha 1-microglobulin in a research communication but contained 15 additional residues.
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| 2. |
- Mendez, E, et al.
(författare)
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Human complex-forming glycoprotein, heterogeneous in charge : the primary structure around the cysteine residues and characterization of a disulfide bridge
- 1982
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Ingår i: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861. ; 213:1, s. 50-240
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Tidskriftsartikel (refereegranskat)abstract
- The amino acid sequence of the cysteine-containing regions of human complex-forming glycoprotein, heterogeneous in charge (protein HC) was determined by studies of the tryptic peptides of the completely reduced and radioalkylated protein. One of the cysteines was located in the amino-terminal part of the molecule at position 34....Diagonal map electrophoresis showed that the cysteine residue in the carboxy-terminal region was bridged to the cysteine containing sequence in the middle of the molecule. The function of the cysteine residue at position 34 remains elusive since the residue was not found on the diagonal maps. The release of cysteic acid and a small cysteic acid containing peptide after oxidation of the native protein HC molecule suggests that this cysteine residue may be involved in disulfide bridges with cysteine and small cysteine containing peptides.
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| 3. |
- Breimer, Michael, 1951
(författare)
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Tissue specificity of glycosphingolipids as expressed in pancreas and small intestine of blood group A and B human individuals.
- 1984
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Ingår i: Archives of biochemistry and biophysics. - 0003-9861. ; 228:1, s. 71-85
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Tidskriftsartikel (refereegranskat)abstract
- A chemical investigation has been done on blood group active glycosphingolipids of both small intestine and pancreas from two individuals, one blood group A and one blood group B. Total non-acid glycolipid fractions were prepared and the major blood group fucolipids present were purified and structurally characterized by mass spectrometry, proton NMR spectroscopy, and degradation methods. The glycolipid structures identified were a blood group Leb hexaglycosylceramide, a B-hexaglycosylceramide with a type 1 (Gal beta 1 leads to 3GlcNAc) carbohydrate chain, A-hexaglycosylceramides with types 1 and 2 (Gal beta 1 leads to 4GlcNAc) carbohydrate chains, a B-heptaglycosylceramide with a type 1 carbohydrate chain, and A-heptaglycosylceramides with type 1 and 2 carbohydrate chains. In addition several minor glycolipids having more than seven sugar residues were detected by thin-layer chromatography. The small intestine and pancreas had some distinct differences in their expression of the major fucolipids. The small intestine contained only glycolipids based upon type 1 carbohydrate chain while the pancreas had both type 1 and type 2 structures. The intestines contained mainly difucosyl compounds while the pancreas tissues contained both mono- and difucosyl glycolipids. Monofucosylglycolipids based on both types 1 and 2 saccharides were present in one pancreas while the other one contained only monofucosylcomponents based on type 1 chain. The ceramides of the intestinal glycolipids were found to be more hydroxylated (trihydroxy long-chain base, hydroxy fatty acids) compared to the pancreas glycolipids (dihydroxy long-chain base, non-hydroxy fatty acids).
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