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  • 1
    Electronic Resource
    Electronic Resource
    Detection of Antibodies in Human Sera to Streptococcal Groups A and C Carbohydrates by a Radioimmunoassay (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 9 (1979), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Human antibodies to Streptococcal groups A and C carbohydrates were measured quantitatively with a radioimmunoassay using tyrosylated 125I carbohydrate. Analysis of acute and convalescent sera from people with groups A or C streptococcal pharyngeal infection or persistent carriage revealed a significant rise in antibodies. Inhibition reactions with the cold carbohydrate indicated the specificity of the elicited antibodies. In some instances, group C as well as group A antibodies occurred after group A pharyngeal infections. Further clinical and epidemiological studies are required to determine the significance of group-specific antibodies. Antistreptolysin-O (ASO) rises were observed in individuals with group C antibody responses after persistent group C pharyngeal carriage. For this reason, epidemiological surveys that rely primarily on ASO surveys to determine the incidence of group A streptococcal infections must be interpreted wilh caution, at least in the developing countries, where group C pharyngeal carriage is common.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1979.tb02707.x
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  • 2
    Electronic Resource
    Electronic Resource
    Complete Amino Acid Sequence of the Variable Domains of Two Human IgM Anti-Gamma Globulins (Lay/Pom) with Shared Idiotypic Specificities (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: On the basis of extensive shared idiotypic specificities, two human IgM anti-gamma-globulins (Lay/Pom) were selected for complete amino acid sequence analysis of their variable domains. Previous studies on the variable regions of the heavy chains of these proteins had shown but eight amino acid differences, only one of which was within a complementarity-determining hypervariable region. The complete amino acid sequence of the variable regions of the light chains of these two proteins is the subject of this report. Protein Lay is a typical VχI protein with only five ‘framework’ differences when compared with protein Roy. Protein Pom is best classified as a VχII, but in the ‘framework’ there are 16 differences between it and protein Ti. Although there are extensive differences in the first hypervariable region, the second and third light-chain hypervariable regions have an identical sequence. The finding of two identical light-chain and two identical heavy-chain hypervariable regions in these two proteins, which were selected on the basis of their combining specificities and their idiotypic cross-reactions, strongly implicates hypervariable regions in the constitution of the idiotypic determinants and the antibody combining site. Additionally, the finding of identical hypervariable regions in light chains of different V-region subgroups fulfills a prediction of the gene-interaction concept of antibody variability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb03017.x
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  • 3
    Electronic Resource
    Electronic Resource
    Structural Studies of Induced Antibodies with Defined Idiotypic Specificities (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The heavy (H) chains of three anti-streptococcal group A carbohydrate antibodies (anti-SACHO) of restricted heterogeneity, elicited in inbred Sprague-Dawley rats, were subjected to 40 cycles of automated Edman degradation. All three antibody H-chain preparations had an identical amino acid sequence and were classified as a variant of the VHIII subgroup of immunoglobulin H chains. A comparison of the H-chain sequence of these antibodies with that of pooled rat gamma chains suggests that a very minor population of H chains (closely related to the VHIII subgroup) has been ‘recruited’ as a consequence of this immunization. This observation further supports the notion that ‘framework’ and ‘specificity’ or “hypervariable regions” are closely linked.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb03043.x
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of the opa (class 5) gene family of Neisseria meningitidis (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 5 (1991), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Class 5 outer membrane proteins of Neisseria meningitidis show both phase- and antigenic variation of expression. The proteins are encoded by a family of opa genes that share a conserved framework interspersed with three variable regions, designated the semivariable (SV) region and hypervariable regions 1 (HV1) and 2 (HV2). In this study, we determined the number and DNA sequence of all of the opa genes of meningococcal strain FAM18, to assess the structural and antigenic variability in the family of proteins made by one strain. Pulsed field electrophoresis and Southern blotting showed that there are four opa genes in the FAM18 chromosome, and that they are not tightly clustered. DNA sequence analysis of the four cloned genes showed a modest degree of diversity in the SV region and more extensive differences in the HV1 and HV2 regions. There were four versions of HV1 and three versions of HV2 among the four genes. Each of the FAM18 opa loci contained a gene with a unique combination of SV, HV1, and HV2 sequences. We used λgt11 cloning and synthetic peptides to demonstrate that HV2 sequences completely encode the epitopes for two monoclonal antibodies specific for different class 5 proteins of FAM18.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1991.tb00789.x
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  • 5
    Electronic Resource
    Electronic Resource
    Localization of a conserved epitope and an azurin-like domain in the H.8 protein of pathogenic Neisseria (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 1 (1987), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The pathogenic neisseriae, Neisseria gonorrhoeae and Neisseria meningitidis, possess an outer membrane protein, H.8, which contains a conserved monoclonal antibody (MAb)-binding epitope in all strains tested. We have cloned and sequenced a meningococcal H.8 gene, and determined the characteristics of the predicted protein. The predicted signal peptide has features characteristic of a prokaryotic lipoprotein. The region at the N-terminal end of the mature protein (39 amino acids) is primarily composed of alanine, glutamate and prollne residues arranged in imperfect repeats with the consensus sequence AAEAP. The epitope for H.8 MAb-binding was localized to a 20-amino acid sequence within this region. The remainder of the predicted amino acid sequence shows extensive homology to azurins, which are small blue copper-binding proteins found in a limited number of species of pathogenic bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1987.tb00510.x
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  • 6
    Electronic Resource
    Electronic Resource
    Genetic and biochemical analyses of protein II (1987)
    Springer
    Antonie van Leeuwenhoek 53 (1987), S. 421-424 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We compared the structure of P.II proteins of gonococcal strain FA1090 by N-terminal sequence analysis of purified proteins and by DNA sequencing of cloned P.II genes. Regulation of P.II gene expression does not involve major DNA rearrangements, but may involve generation of frame-shifts in unexpressed P.II genes. There are probably 8 or 9 P.II genes, each possessing a common leader sequence, in the gonococcal chromosome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00415496
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  • 7
    Electronic Resource
    Electronic Resource
    Fast atom bombardment/tandem mass spectrometry of physalaemin-like peptides (1987)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 14 (1987), S. 281-287 
    Details
    ISSN: 0887-6134
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Fragment ion spectra obtained from collision-induced decomposition of protonated molecular ions have been used to determine amino acid sequences of several physalaemin-like peptides which were recently purified from rabbit stomach. This technique was chosen because the peptides were available in microgram quantities and were anticipated to contain pyroglutamate as the blocked N-terminal residue. Such spectra of several synthetic analogs of the naturally occurring peptides were obtained and analyzed to confirm the veracity of this peptide sequencing strategy. In addition, methyl ester derivatives of these synthetic peptides provided a crucial test for the spectral interpretation via the mass shifts thus induced.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200140607
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  • 8
    Electronic Resource
    Electronic Resource
    Effect of proteolytic enzymes on vaccinia virus replication (1969)
    Springer
    Archives of virology 26 (1969), S. 321-333 
    Details
    ISSN: 1432-8798
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Chymotrypsin and trypsin enhance vaccinia virus replication in chick embryo cell cultures. Two phenomena are described: an enhancement of plaque numbers and an increase in plaque size. Low doses of chymotrypsin (1.3μg/4 million cells) acting on the virus particles are responsible for the increase in vaccinia virus plaque numbers. The effect is not due to disaggregation of virus aggregates by the enzyme. Doses of 3 to 10 (μg of chymotrypsin per culture have an effect on chick embryo cell monolayers. A linear dose response is found when plaque size is measured as a function of the dose of chymotrypsin. Preliminary studies indicate that some of the enzyme becomes cell-associated. When one replication cycle was followed the final yield of plaque forming virus from both enzyme treated and control cells was the same. However, the process of replication in enzyme treated monolayers was accelerated by about 5 hours. The enzyme appears to have an effect on some early event in virus replication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01250942
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