SEQUENCE COMPARISON OF HUMAN PLASMA α1‐ACID GLYCOPROTEIN AND THE IMMUNOGLOBULINS
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Abstract:
The amino acid sequence of human plasma α 1 ‐acid glycoprotein, upon comparison with the sequences of other blood proteins, was shown to possess significant similarity with the immunoglobulins. Employing direct and corrected sequence identity, the average mutation value and two different computer comparisons for the evaluation of sequence similarity, the following two regions of this α‐globulin, which account for approximately half of the total amino acid sequence of the protein, were found to possess sequence similarity with the immunoglobulins. a) The region from residues 77 through 125 proved to be related to the variable region of several human H and L chains, and b) the region from residues 136 through 166 was found to be related not only to the constant region of a human and a mouse L chain but also to the third and fourth constant region of a rabbit and a human H chain, respectively. These results suggest that α 1 ‐acid glycoprotein is probably related to the immunoglobulins and further suggest that it possibly diverged from the immunoglobulin evolutionary tree prior to the formation of the primitive L chain.Keywords:
Sequence (biology)
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Antibodies were raised in rabbits against purified swine and human trachea and Cowper's gland mucin glycoproteins and their deglycosylated polypeptide chains. Three monospecific antibody fractions that recognize the carbohydrate, the deglycosylated or unglycosylated regions of the polypeptide chains in these glycoproteins, were isolated by immunoaffinity chromatography. The human and swine trachea mucin glycoproteins showed extensive immunological homology in both their carbohydrate and polypeptide chains. The carbohydrate chains and unglycosylated region of the polypeptide chain in Cowper's gland mucin glycoprotein showed little or no cross-reaction with comparable regions in respiratory mucin glycoproteins. However, the polypeptide chains in the deglycosylated regions of all three mucin glycoproteins showed extensive homology. Five bands with molecular masses ranging from 40 to 46 kDa that differed by a constant molecular mass of approximately 1.5 kDa were detected in hydrolysates of all of the polypeptide chains after treatment with S. aureus V8 protease. Monospecific antibodies to the deglycosylated region of these chains reacted with the peptides, whereas those directed against the unglycosylated region did not. The results suggest that these chains contain tandem repeating sequences of amino acids.
Molecular mass
Homology
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Herpes simplex virus (HSV) is one of the infecting human viruses. To achieve the entry of virion into the host cells, HSV requires 5 types of the glycoprotein, which are glycoprotein C (gC), glycoprotein D (gD), Glycoprotein B (gB) and a complex of glycoprotein H and glycoprotein L (gH-gL). All five glycoproteins are mandatory for HSV-host interaction and infection. There will be no invasion to the cells without involvement of these glycoproteins; there will be no cellular invasion. In this paper, we aligned the nucleotide sequences of glycoprotein B and glycoprotein D from herpes simplex types l & 2 virus. By comparing these nucleotide sequences between herpes simplex type l and type 2 viruses, we able to find out the conserved and non-conserved regions, which indicate the similarities and differences between glycoprotein B and glycoprotein D of these two human herpes viruses.
Herpesvirus glycoprotein B
Membrane glycoproteins
Simplexvirus
P-glycoprotein
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Membrane glycoproteins
Endoglycosidase H
Oligosaccharide
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The cerebellar glycoproteins of bovine have been separated by affinity chromatography on Con A-Sepharose and analyzed by poliacrylamide gel electrophoresis. Some soluble Con A binding glycoproteins are common to the insoluble (membrane bound) glycoproteins suggesting a relationship between the two classes of molecules. The data support the hypothesis that some of the soluble glycoproteins can be considered precursors of the insoluble.
Membrane glycoproteins
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Herpes simplex virus type 2-specific glycoproteins present in detergent extracts of infected cells were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under conditions designed to permit detection of multimeric forms of these glycoproteins. Two high-molecular-weight glycosylated species were detected when samples were disrupted at lower temperatures or in the absence of any reducing agents. One multimer having an apparent molecular weight of 275,000 was identified as a multimer of the gA or gB glycoprotein or both. The second glycoprotein, having a molecular weight of approximately 230,000, was identified as a multimeric form of the gC glycoprotein. These data indicate that the gC as well as the gA and gB glycoproteins of herpes simplex virus type 2 may exist in a multimeric form.
Sodium dodecyl sulfate
Membrane glycoproteins
Herpesvirus glycoprotein B
Molecular mass
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The mucous glycoproteins are the components of the mucous secretions of the internal passages of higher animals that cause the high viscosity of the secretions, and they may be responsible for many immunological phenomena. Although the number of highly purified mucus glycoproteins is still limited, evidence suggests that they are tissue and species specific in their composition and reactions. They seem to be related closely to the glycoproteins and glycolipids of cell membranes. In the development of their structures, the use of alkalies has provided valuable information but improperly used has caused several misinterpretations. The glycoproteins are composed of a protein core to which are attached numerous oligosaccharides. Studies of the primary structure of bovine submaxillary glycoprotein show that it consists of many covalently bound repetitive sequences of short peptides of similar composition. Other mucus glycoproteins seem to have similar primary structures for the protein core.
Core protein
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BHK cells infected with strain 17 syn+ (HSV-1) or HG52 (HSC-2) incorporated inorganic sulphate into polypeptides which co-migrated on SDS-polyacrylamide gels with virus-induced glycoproteins. The major sulphated glycoprotein was glycoprotein E. In addition, less-intense sulphated bands co-migrated with glycoprotein D and HSV-1 glycoprotein A/B/C. Sulphate label co-migrating with HSV-2 glycoprotein A/B/C was occasionally observed. We have investigated which sulphated polypeptides are excreted from infected cells. Major ones of apparent mol. wt. 32000, 34000 and 35000 were excreted from cells infected with syn+. In addition, polypeptides which migrated in the vicinity of glycoprotein D were often excreted from cells infected with either 17 syn+ or HG52. The 32K, 34K and 35K polypeptides were antigenically related to glycoprotein D and over 95% of the total amount synthesized was excreted. Analysis of intracellular sulphated polypeptides using intertypic recombinants mapped glycoprotein E to between 0.832 and 0.950 units of the HSV genome.
Herpesvirus glycoprotein B
P-glycoprotein
Membrane glycoproteins
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