Hans Erik Carlsson

Immunological studies in ulcerative colitis. VIII. Antibodies to colon antigen in patients with ulcerative colitis, Crohn's disease, and other diseases.

Sera from patients with ulcerative colitis or Crohns disease had elevated titers to colon antigen from germ-free rats significantly more often than sera from patients with gastroenteritis, irritable colon, non-gastrointestinal diseases, and healthy controls. Elevated anticolon titers in significant frequency were also found in patients with liver cirrhosis, urinary tract infections, and in polyposis coli and their relatives. Females with ulcerative colitis had, on an average, higher titers than men especially in the age group 30 years and over. In Crohns disease the antibody titers often increased with time--as opposed to those in ulcerative colitis and non-gastrointestinal diseases. In conjunction with results published earlier, the present work supports the assumption that the antibodies in ulcerative colitis patients react with antigenic determinants distinct from those recognized by the colon antibodies present in other groups, including patients with Crohns disease and polyposis.

Quantitation of Salmonella O-Antibodies in Human Sera by Enzyme-Linked Immunosorbent Assay (ELISA)

The enzyme-linked immunosorbent assay (ELISA) has been applied to the detection of antibodies against Salmonella O-antigens in human sera. Phenol-water extracted lipopolysaccharides (LPS) from serogroups A (O-antigens 2, 12), B (4, 5, 12) and D (9, 12) were used as antigens. When compared to the tube agglutination method according to Widal employing sera from patients with verified or suspected typhoid--or paratyphoid fever and from healthy controls it was found that ELISA (i) correlated significantly with the Widal reaction, (ii) was up to 100-fold more sensitive, and (iii) showed a greater reproducibility.

Artificial diaccharide-protein conjugates as immunogens for the preparation of specific anti-salmonella O-antisera

Abstract Disaccharides representing the antigenic determinants of the O-antigenic polysaccharide chain of Salmonella serogroups B and D were synthesized, and covalently linked to bovine serum albumin as the immunogenic carrier. Rabbits, immunized with these artificial antigens, produced antisera which were shown by passive hemagglutination and complement-midiated bactericidal assays, to be specific and superior to conventional antisera. When used in indirect immunofluoresence tests for the identification of Salmonella bacteria, the antisera also proved highly specific, correctly identifying all of the isolates.

Structure of some oligosacharides derived from rat-intestinal glycoproteins

Glycoproteins derived from intestinal mucus were isolated by phenol-water extraction of feces from germ-free rats. The water-soluble glycoproteins were subjected to alkaline-borohydride degradation, and three different oligosaccharide alditols were isolated. The structures of thse were determined by using methylation analysis and n.m.r. spectroscopy as the principal methods. One disaccharide alditol and one trisaccharide alditol were characterised as beta-D-GlcNAcp-(1 leads to 3)-D-GalNAcol and alpha-L-Fucp-(1 leads to 2)-beta-D-Galp-(1 leads to 3)-D-GalNAcol. The third oligosaccharide alditol was a blood-group A-active tetrasaccharide alditol for which the structure alpha-D-GalNAcp-(1 leads to 3)-[alpha-L-Fucp-(1 leads to 2)]-beta-D-Galp-(1 leads to 3)-D-GalNAcol is proposed.

Immunochemistry of Salmonella O-antigens. Specificity and cross-reactivity of factor O9 serum and of antibodies against tyvelose (Formula: see text) mannose coupled to bovine serum albumin.

The octasaccharide Galp (Formula: see text) Rhap, the synthesized disaccharides methyl 3-O-a-tyvelopyranosyl-a-D-mannopyranoside, methyl 3-O-a-tyvelopyranosyl-beta-D-mannopyranoside and methyl alpha-tyveloside, in order of decreasing effectiveness, inhibited the precipitation of S. typhi T2 alkali-treated lipopolysaccharide by O-factor 9 serum. On a molar basis the relative inhibiting activities of the glycosides were by O-factor 9 serum. On a molar basis the relative inhibiting activities of the glycosides were 100:22:8:2. With rabbit aniserum raised against 3-O-a-tyvelopyranosyl-D-mannopyranosyl covalently linked to bovine serum albumin the relative inhibitory activities of the four glycosides were 11:100:26:3. These data establish that the 3-O-a-tyvelopyranosyl-a-D-mannopyranosyl structure is immunodominant in the Salmonella O-antigen 9. The specificity of the antigen-antibody interaction was high: glycosides in which the tyvelose (3,6-dideoxy-D-arabino-hexose) residue had been replaced by abequose (3,6-dideoxy-D-xylo-hexose) or paratose (3,6-dideoxy-K-ribo-hexose), had less than one fiftieth of the activity of the most active inhibitor in either of the two precipitation systems used. Moreover, the results show that 3-O-a-tyvelopyranosyl-D-mannopyranosyl coupled to bovine serum albumin elicits O-antibodies of higher specificity than those obtained by absorption of antibacterial immune serum.

Isoelectric Focusing and Immunological Characterization of Human Serum Albumin

Publisher Summary Human serum albumin (HSA) is known to be a relatively homogeneous protein. This chapter describes the isoelectric focusing and immunological characterization of human serum albumin. HAS was electrofocused in electrofocusing equipment using a column of 100 ml volume. It is found that as the isoelectric point of HSA is pH 4.9, carrier ampholytes covering the pH range 4–6 were chosen. The absorbancy of the effluent was measured in a spectrophotometer at 280 nm. To exclude contribution by the carrier ampholytes, it was necessary to perform electrofocusing without sample. Within the range of the pH gradient, the absorbancy of such a run at 280 nm was low. The recovery of protein was quantitated spectrophotometrically at 280 nm and also by radial diffusion according to Mancini. In the latter experiments, a 1 % gel of Difco Special Agar Noble mixed with the appropriate amount of antiserum was used. The recovery of HSA was also established by quantitative immunoelectrophoresis