Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “LACTOGLOBULINS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 541 records · Page 30Linked to original sources

Characterization of genetic polymorphism in the goat beta-lactoglobulin gene.

Two new variants have been detected and characterized for the goat beta-lactoglobulin gene at the cDNA level and confirmed at the genomic level. The two polymorphisms are located on exon 7 of the gene. One of the polymorphic sites is produced by a single nucleotide substitution in position +4601, allowing a polymerase chain reaction--restriction fragment length polymorphism (PCR-RFLP) genotyping procedure to be developed using SacII restriction enzyme. The other polymorphic position contains a 10 bp long insertion at position +4641 that can be detected by capillary electrophoresis of the PCR product amplified with a fluorescent primer. The association of these two polymorphisms was also investigated, resulting in the description of two new alleles. Both of these contained the point mutation at the SacII site, with or without the 10 bp insertion at position +4641. The distribution of these new polymorphisms was studied in a population of males of four different goat breeds. The gene frequencies for these variants were similar in Spanish and French breeds.

Alleles↗

Heat stability in concentrated and non-concentrated milks--the effect of urea and beta-lactoglobulin levels and the influence of preheating.

Heat stability as a function of pH has been studied in concentrated and non-concentrated milk systems. The influence of preheating has also been examined. The concentration of beta-lactoglobulin has been shown to affect markedly the heat stability behaviour in both systems but with different characteristics. Increasing the level of urea resulted in increased heat stability in non-concentrated milks, but corresponding concentrated milks showed a small decrease in maximum heat stability. It has not been possible to extrapolate heat stability data from non-concentrated to concentrated milks.

Animals↗

Heat-induced association of beta-lactoglobulin and casein micelles.

Heat-induced association of beta-lactoglobulin (beta-lg) and casein micelles, mainly at 85--90 degrees C, was studied by means of preparative ultracentrifugation, using [3H]-labelled beta-lg. Qualitative aspects were studied by gel electrophoresis and electron microscopy. In this association, the formation of intermolecular S-S bonds between beta-lg and kappa-casein plays a role, but hydrophobic bonds are also involved. After heating mixtures containing 25 g/kg casein and 4 g/kg beta-lg at 90 degrees C for 20 min, the amount of beta-lg sedimented with the casein micelles by ultracentrifugation decreased by approximately 30% when the milk salt buffer system was reduced to 0.25 of its normal concentration; it decreased by about 20% when the pH was increased from 6.8 to 7.3 and increased by 15% when the pH was reduced from 6.8 to 5.8. When the beta-lg concentration was decreased from 4 to 2 g/kg, the amount of sedimented beta-lg decreased by 25% after heating at 90 degrees C for 6 min. After heating in milk salt buffer, the amount of sedimented beta-lg was 15% higher than after heating in salt solution which contained neither Ca nor citrate ions. Although alpha-lactalbumin (alpha-la) is involved in the heat-association of beta-lg and casein micelles, no influence of alpha-la on the amount of associated beta-lg was found. In addition to the heat-association product of beta-lg and whole casein micelles, an association product consisting mainly of beta-lg and kappa-casein was also formed. This product was observed by electron microscopy as noodle-like particles. The size of these particles depended on the beta-lg/kappa-casein ratio.

Animals↗

Does beta-lactoglobulin occur in human milk?

Although beta-lactoglobulin (beta-lg) has been considered to be absent from human milk, recent results of other workers, based on immunological reactions between human milk and rabbit antiserum to bovine beta-lg, suggest that this protein may be present. Although our results show similar immunological reactions, we consider that lactoferrin is responsible for these, as it was the only reactive protein species which could be prepared to homogeneity. Indeed two types of antibodies were found by ELISA test in the antisera to bovine beta-lg. One of them would be able to bind loosely to human lactoferrin, but its binding sites would not be antigenic in the rabbit.

Animals↗

Effect of high hydrostatic pressure on the enzymic hydrolysis of beta-lactoglobulin B by trypsin, thermolysin and pepsin.

Hydrolysis of beta-lactoglobulin B (beta-lg B) by pepsin, a process slow at ambient conditions, is facilitated at a moderately high hydrostatic pressure such as 300 MPa, corresponding to an apparent volume of activation delta V# = -63 ml mol-1 at pH 2.5, 30 degrees C and gamma/2 = 0.16. Digestion of beta-lg by trypsin and thermolysin is likewise enhanced by pressure, and the pressure effect has been traced to pressure denaturation of beta-lg B, which by high-pressure fluorescence spectroscopy has been shown to have a large negative volume of reaction, delta V(o) = -98 ml mol-1, at pH 6.7, 30 degrees C and gamma/2 = 0.16. Pressure denaturation is only slowly reversed following release of pressure and the enhanced digestibility is maintained at ambient pressure for several hours.

Hydrolysis↗

Goats' milk of defective alpha(s1)-casein genotype decreases intestinal and systemic sensitization to beta-lactoglobulin in guinea pigs.

Contradictory results have been reported on the use of goats' milk in cows' milk allergy. In this study the hypothesis was tested, using a guinea pig model of cows' milk allergy, that these discrepancies could be due to the high genetic polymorphism of goats' milk proteins. Forty guinea pigs were fed over a 20 d period with pelleted diets containing one of the following: soyabean proteins (group S), cows' milk proteins (group CM), goats' milk proteins with high (group GM1) or low (group GM2) alpha(s1)-casein content. Parenteral sensitization to GM1 and GM2 proteins as also assessed. The sensitization was measured (1) by systemic IgG1 antibodies directed against bovine or caprine beta-lactoglobulin (beta-lg), alpha-lactalbumin (alpha-la) and whole caseins, and (2) by intestinal anaphylaxis measured in vitro in Ussing chambers, by the rise in short-circuit current (delta Isc) in response to milk proteins. Guinea pigs fed on CM and GM1 developed high titres (> 1500) of anti-beta-lg IgG1, with an important cross reactivity between goat and cow beta-lg. However, in guinea pigs fed on GM2, anti-goat beta-lg IgG1 antibodies were significantly decreased compared with GM1 guinea pigs (mean IgG1 titres were 546 and 2046 respectively), and the intestinal anaphylaxis was significantly decreased (3.5+/-4.5 microA/cm2) compared with that observed in GM1 guinea pigs (8.3+/-7.6 microA/cm2). Animals receiving GM1 or GM2 proteins via the parenteral route developed a marked sensitization. These results suggest that the discrepancies observed in the use of goats milk in cows' milk allergy could be due, at least in part, to the high genetic polymorphism of goats' milk proteins.

Anaphylaxis↗

Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment.

Bovine beta-lactoglobulin (beta-lg), alpha-lactalbumin (alpha-la) and bovine serum albumin (BSA), dispersed in ultrafiltration permeate, that had been prepared from whey protein concentrate solution (100 g/kg, pH 6.8), were heated at 75 degrees C. The sequent protein aggregation was studied by one-dimensional (1D) and two-dimensional (2D) polyacrylamide gel electrophoresis (PAGE). When 100 g beta-lg/kg permeate solution was heated at 75 degrees C, cooled and examined, large aggregates were observed. These aggregates were partially dissociated in SDS solution to give monomers, disullphide-bonded dimers, trimers and larger aggregates. When mixtures of beta-lg and alpha-la or BSA were heated, homopolymers of each protein as well as heteropolymers of these proteins were observed. These polymer species were also served in a heated mixture of the three proteins. Two-dimensional PAGE of mixtures demonstrated that these polymers species contained disulphide-bonded dimers of beta-lg. alpha-la and BSA, and 1:1 disulphide-bonded adducts of alpha-la and beta-lg, or BSA. These results are consistent with a mechanism in which the free thiols of heat-treated beta-lg or BSA catalyse the formation of a range of monomers, dimers and higher polymers of alpha-la. It is likely that when whey protein concentrate is heated under the present eonditions. BSA forms disulphide-bonded strands ahead of beta-lg and that alpha-la aggregation with beta-lg and with itself is catalysed by the heat-induced unfolded BSA and beta-lg.

Animals↗

Effect of beta-lactoglobulin on plasma retinol and triglyceride concentrations, and fatty acid composition in calves.

Beta-lactoglobulin (beta-lg) is the main protein of ruminant milk whey. Although beta-lg can bind in vitro to a variety of hydrophobic substrates, mainly retinol and long-chain fatty acids, its physiological function is still unknown. In Exp. 1, we investigated the effect of beta-lg on the plasma retinol concentration in preruminant calves. Holstein male calves (n = 20) were fed Holstein whole milk at 40 g/kg body weight (BW) plus vitamin A acetate (500,000 i.u.) with or without beta-lg (0.4 g/kg BW). The plasma retinol concentration of 10-d-old calves was greater (P < 0.05) in the beta-lg-fed group) than in the control group during the period from 8 to 12 h and at 24 h after the feeding. The postprandial change of plasma retinol in 40-d-old calves fed milk with beta-lg was higher (P < 0.05) than that in the control calves only at 12 h after the feeding. In Exp. 2, Holstein male calves (n = 18) were used to investigate the effect of beta-lg on plasma triglyceride concentration and fatty acid composition. Calves were fed Holstein whole milk at 40 g/kg BW plus milk fat prepared from whole milk at 2 g/kg BW with or without beta-lg (0.4 g/kg BW). Plasma triglyceride concentration at age 10 d was higher (P < 0.05) in the beta-lg-fed group than in the controls during the periods from 1 to 2 h and from 7 to 11 h after the feeding. At age 40 d, plasma triglyceride in the beta-lg-fed group was higher (P < 0.05) than in the control group only at 9 h. Ratios of palmitic, stearic, and oleic acids to total plasma lipids were higher (P < 0.05) in the calves fed beta-lg milk than in the control calves at age 10 d. These results suggest that beta-lg enhances the intestinal uptake of retinol, triglyceride, and long-chain fatty acids in preruminant calves.

Animals↗

Caprine immunoglobulin G, beta-lactoglobulin, alpha-lactalbumin and serum albumin in colostrum and milk during the early post partum period.

Colostrum and milk samples from 20 goats were analysed for concentrations of immunoglobulin G (IgG), beta-lactoglobulin (beta-lg), alpha-lactalbumin (alpha-la) and serum albumin (CSA) throughout the first 14 milkings post partum (7 d of lactation) using single radial immunodiffusion assay. Concentrations (mg/ml, means +/- SD) at first milking were IgG 47.9 +/- 25.5, beta-lg 30.7 +/- 10.4, alpha-la 2.77 +/- 0.82 and CSA 2.97 +/- 2.46 mg/ml. Large variations were recorded for IgG concentrations (19.9-94.5 mg/ml) and beta-lg (9.3-49.8 mg/ml). Concentrations of IgG, beta-lg and CSA dropped abruptly in the subsequent milkings and alpha-la concentration decreased slowly. Mean IgG concentration was < 2 mg/ml after 7 milkings and < 1 mg/ml after 11 milkings. However, IgG concentration does not differ significantly, at the 1% level, from milkings 7-14. The contribution of beta-lg to the increase in whey proteins in early milks was greater than that of IgG from milkings 5 to 14. The results were tabulated to make it possible to calculate the excess of whey proteins that would be obtained if early milks were illegally added to milk supply.

Animals↗

Heat-induced interactions of beta-lactoglobulin A and kappa-casein B in a model system.

The interaction of kappa-casein and beta-lactoglobulin is fundamental to all heat-induced modifications of milk product functionality, such as the heat stability of concentrated milks. Purified native kappa-casein B and beta-Ig A solutions were heated at 80 degrees C at pH 6.7 separately and in a mixture. The circular dichroism spectra in the near UV indicated irreversible changes in the disulphide bonding patterns involving both proteins. Alkaline- and SDS-PAGE of heated samples showed that, in the presence of kappa-casein, less beta-Ig was converted into beta-Ig polymers and the rate of loss of native beta-Ig was greater. When kappa-casein was added to previously heated beta-Ig and the mixture was heated, the kappa-casein reacted with the heat-induced beta-Ig polymers more readily than with the beta-Ig native monomers. The formation of beta-Ig dimers, trimers etc. was diminished. It was concluded that, when beta-Ig and kappa-casein were heated together, beta-Ig formed thiol-exposed monomers, which reacted with each other or with the native kappa-casein depending on the relative concentrations of beta-Ig and kappa-casein. The products of these reactions included some disulphide-bonded 1:1 beta-Ig:kappa-casein complexes, some monomer kappa-casein and a range of large aggregates held together by either or both disulphide bonds and hydrophobic association.

Caseins↗

Kinetics of alkaline phosphatase and lactoperoxidase inactivation, and of beta-lactoglobulin denaturation in milk with different fat content.

In the context of identifying intrinsic time temperature integrators (TTIs) for evaluating heat processing of milk, the extent to which milk fat content has an effect on alkaline phosphatase (ALP) and lactoperoxidase (Lpo) inactivation and on beta-lactoglobulin (beta-Ig) denaturation kinetics was studied. Inactivation and denaturation kinetics were analysed in whole, semi-skimmed and skimmed milk. In previous experiments (isothermal and non-isothermal heating conditions), heat inactivation of ALP and Lpo and heat denaturation of beta-Ig were found to follow first order kinetics. This allowed experimental design to be simplified. Data analysis was performed by non-linear regression and results were evaluated by construction of joint confidence regions. The possible effect of milk fat was illustrated by temperature time tolerance (TTT-) diagrams. Although initial ALP activity was lower in skimmed milk compared with semi-skimmed or whole milk, kinetics were comparable and fat content did not seem to substantially affect the ALP test result for pasteurized milk. Unlike ALP, Lpo inactivation and beta-Ig denaturation kinetics differed significantly in milk with different fat content. Differences between Lpo inactivation kinetics were relatively small and acceptable in the context of quantifying the process impact. Denaturation of beta-Ig, on the other hand, seemed to be enhanced at higher milk fat content (> 72 degrees C).

Alkaline Phosphatase↗

Thermal stability of beta-lactoglobulins A and B: effect of SDS, urea, cysteine and N-ethylmaleimide.

Fourier transform infrared spectroscopy (FTIR) and differential scanning calorimetry (DSC) were used to monitor changes in the secondary structure and thermal stability of beta-lactoglobulin A and B in the presence of sodium dodecyl sulphate (SDS), N-ethylmaleimide (NEM), urea and cysteine. An increase in the thermal stabilities of both proteins was noted in the presence of 10 mM-SDS. In the presence of 50 mM-SDS, there was extensive denaturation of both variants. In general, the beta-strand/beta-sheet regions in the secondary structure of both variants were very susceptible to denaturation by SDS and cysteine, suggesting that these regions may be held by hydrophobic and disulphide bonds. At ambient temperature and physiological pH, a notable difference was observed in the 1636 and 1627 cm(-1) regions of the FTIR spectra of the two beta-lg variants. The results suggest possible differences in the nature of the beta-sheet/beta-strand distribution/ content of the two proteins. Urea and NEM at a concentration of 50 mM, had little effect on the secondary structure and denaturation of both variants. New findings are presented which further indicate that although the beta-lg B variant showed greater thermal stability than the A variant in all the cases studied, its denaturation temperature and secondary structure were affected to a greater extent by the protein perturbants than beta-lg A.

Calorimetry, Differential Scanning↗

High pressure-induced denaturation of alpha-lactalbumin and beta-lactoglobulin in bovine milk and whey: a possible mechanism.

In this study, high pressure (HP)-induced denaturation of alpha-lactalbumin (alpha-la) and beta-lactoglobulin (beta-lg) in dairy systems was examined. In both milk and whey, beta-lg was less baroresistant than alpha-la; both proteins were considerably more resistant to HP-induced denaturation in whey than in milk. HP-induced denaturation of alpha-la and beta-lg increased with increasing proportion of milk in mixtures of milk and whey. Addition of a sulphydryl-oxidising agent, KlO3, to milk or whey increased HP-induced denaturation of beta-lg, but reduced the denaturation of alpha-la. Denaturation of both alpha-la and beta-lg was prevented by adding a sulphydryl-blocking agent, N-ethylmaleimide, to milk or whey prior to HP treatment, highlighting the crucial role of sulphydryl-disulphide interchange reactions in HP-induced denaturation of alpha-la and beta-lg. Removal of colloidal calcium phosphate from milk also reduced HP-induced denaturation of alpha-la and beta-lg significantly. The higher level of HP-induced denaturation of alpha-la and beta-lg in milk than in whey may be the result of the abscence of the casein micelles and colloidal calcium phosphate from whey, which facilitate HP-induced denaturation of alpha-la and beta-lg in milk.

Animals↗

Influence of high hydrostatic pressure on the proteolysis of beta-lactoglobulin A by trypsin.

This work describes the effect of the hydrolysis time and pressure (0.1-400 MPa) on the proteolysis of beta-lactoglobulin A (beta-lg A) with trypsin, either conducting hydrolysis of beta-lg under pressure or hydrolysing beta-lg that was previously pressure treated. Pressurisation, before or during enzyme treatments, enhanced tryptic hydrolysis of beta-lg. Trypsin degraded pressure-modified beta-lg and pressure-induced beta-lg aggregates, favouring proteolysis to the intermediate degradation products: (Val(15)-Arg(40)), (Val(41)-Lys(69))S-S(Leu(149)-Ile(162)) and (Val(41)-Lys(70))S-S(Leu(149)-Ile(162)). These were further cleaved at the later stages of proteolysis to yield: (Val(15)-Tyr(20)), (Ser(21)-Arg(40)), (Val(41)-Tyr(60)), (Trp(61)-Lys(69))S-S(Leu(149)-Ile(162)) and (Trp(61)-Lys(70))S-S(Leu(149)-Ile(162)). Particularly, in the tryptic hydrolysates of pre-pressurized beta-lg, two other fragments linked by disulphide bonds: (Lys(101)-Arg(124))S-S(Leu(149)-Ile(162)) and (Tyr(102)-Arg(124))S-S(Leu(149)-Ile(162)), were found. These corresponded to rearrangement products induced by SH/SS exchange between the free thiol group of Cys(121) and Cys(160), that normally forms the disulphide bond Cys(66)-Cys(160). In the light of these results, structural modifications of beta-lg under high pressure are discussed.

Animals↗

Genetic variants of beta-lactoglobulin gene and its association with milk composition traits in riverine buffalo.

A study was carried out to determine genetic variants of beta-lactoglobulin gene and to explore associations between these and milk composition traits in riverine buffalo. Single strand conformation polymorphism was employed to detect the genetic variants of the gene. Two fragments of this gene i.e. 119 bp of exon I and 400 bp spanning exon IV and intron IV were included in the study. For 119 bp fragment, three alleles namely, A, B and C were observed in all the buffalo breeds whereas four alleles (A, B, C and D) were detected for 400 bp fragment. The frequency distribution of alleles was different in different breeds of buffaloes for both the fragments. For exon I fragment, the milk composition traits such as total SNF, protein, solid, fat and whey protein yield were found to be significantly (P<0.05) associated with genotypes in Murrah and Bhadawari buffalo whereas in Mehsana breed genotypes were significantly (P<0.05) co-related with total SNF, solid and fat yield. Genotypes of 400 bp fragment, only total fat yield in Mehsana buffalo was found to be significantly (P<0.05) associated with genotypes.

Alleles↗

Bovine immunoglobulin G, beta-lactoglobulin, alpha-lactalbumin and serum albumin in colostrum and milk during the early post partum period.

Colostrum and milk samples from 60 Holstein-Friesian cows were analysed for concentrations and yields of immunoglobulin G (IgG), beta-lactoglobulin (beta-lg), alpha-lactalbumin (alpha-la) and serum albumin (BSA) throughout the first 16 milkings post partum (8 d of lactation) using a single radial immunodiffusion assay. Concentrations (mg/ml, means +/- SD) at first milking were IgG 59.8 +/- 28.5, beta-lg 14.3 +/- 4.6, alpha-la 2.04 +/- 0.6, BSA 1.21 +/- 0.44. Large variations were recorded for IgG concentrations (15.3-176.2 mg/ml) and yields (0.2-925 g). Cows in their first lactation produced significantly lower concentrations and yields of colostral IgG than cows in later lactations. A colostral yield of IgG below the 100 g required to prevent calf hypo-gamma-globulinaemia was found in 18.3% of the cows. The concentrations of IgG, beta-lg and BSA dropped abruptly in subsequent milkings and alpha-la concentration decreased slowly. The mean IgG concentration was < 2 mg/ml after eight milkings and < 1 mg/ml after fifteen milkings. However, IgG concentration did not differ significantly, at the 1% level, during milkings 11-15. The results were tabulated to make it possible to calculate the excess of whey proteins that would be obtained if early milks were illegally added to the milk supply.

Animals↗

Pressure denaturation and aggregation of beta-lactoglobulin studied by intrinsic fluorescence depolarization, Rayleigh scattering, radiationless energy transfer and hydrophobic fluoroprobing.

beta-Lactoglobulin (beta-lg) in aqueous solution under pressure showed a marked depolarization of intrinsic fluorescence assigned to a gradually increased rotational diffusion of tryptophyl moieties in pressure-unfolded states. The corresponding change in anisotropy provided a new and more accurate method for determining denaturation volume which, for beta-lg in neutral aqueous solution with ionic strength 0.16 (NaCl) at 25 degrees C, was delta V degree = -73 (SE 3) ml mol-1, corresponding to half denaturation at 123 MPa. The pressure unfolding led to exposure of hydrophobic regions to the protein-water interface that could be probed by fluorescence intensity of a beta-lg-1-anilinonaphthalene-8-sulphonic acid (ANS) complex with 1:1 stoichiometry, as determined by Job's method of continuous variation. The unfolding of beta-lg impaired the binding capacity of the inner calyx, with a reduction in binding capacity of 50% at 50 MPa, as shown by decreasing cis-parinaric acid fluorescence, decreasing anisotropy and decreasing radiationless energy transfer from tryptophans to this probe with increasing pressure. The pressure-induced reversible exposure of hydrophobic groups to the protein-water interface may, at least partly, explain the initial aggregation reactions, evident from increased Rayleigh scattering from approximately 50 MPa, prior to irreversible pressure-induced gel formation of beta-lg. Using results from this and previous studies, we propose a three step pressure denaturation model for beta-lg for neutral solution at ambient temperature, including an initial pressure-melted state (up to 50 MPa) with partial collapse of the inner calyx and solvent exposure of the free thiol group, followed by a reversible denaturation with exposure of hydrophobic regions (half denaturation at 123 MPa) and with irreversible denaturation with thiol-disulphide exchange becoming increasingly important at higher pressures. Effects of pressure on beta-lg, as measured by fluorescence depolarization, were found for the reversible denaturation steps to be similar to the effects of chemical denaturants but different with respect to shift in ANS emission maxima.

Anilino Naphthalenesulfonates↗

Modulation of the T cell response to beta-lactoglobulin by conjugation with carboxymethyl dextran.

We have previously prepared beta-lactoglobulin (beta-LG)-carboxymethyl dextran (CMD) conjugates with water-soluble carbodiimide and achieved reduced immunogenicity of beta-LG. In the present study, to elucidate the mechanism for the reduced immunogenicity of beta-LG, we investigated changes in the T cell response to beta-LG after conjugation with CMDs differing in molecular weight (about 40 and 162 kDa). Lymph node cells from BALB/c, C3H/He, and C57BL/6 mice that had been immunized with beta-LG or the conjugates were stimulated with beta-LG, and the in vivo T cell response was then evaluated by BrdU (5-bromo-2'-deoxyuridine) ELISA as the ex vivo proliferative response. T cells from the conjugate-immunized mice showed a lower proliferative response than those from the beta-LG-immunized mice. T cell epitope scanning, using synthesized peptides, showed that the T cell epitope profiles of the conjugates were similar to those of beta-LG, whereas the proliferative response to each epitope was reduced. These results indicate that the lower in vivo T cell response with the conjugates was not due to induction of conjugate-specific T cells, but due to a decrease in the number of beta-LG-specific T cells. After the lymph node cells from beta-LG-immunized mice had been stimulated with beta-LG or the conjugates, the efficiency of the antigen presentation of the conjugate to beta-LG-specific T cells was evaluated by BrdU ELISA as the in vitro proliferative response. The antigen presentation of beta-LG to the T cells was reduced by conjugation with CMD. In addition, conjugation with CMD enhanced the resistance of beta-LG to cathepsin B and cathepsin D, which suggest that conjugation with CMD inhibited the degradation of beta-LG by proteases in APC and led to suppression of the generation of antigenic peptides including T cell epitopes from beta-LG. It is therefore considered that the suppressive effect on the generation of T cell epitopes reduced the antigen presentation of the conjugates and that this reduction led to a decrease in the number of beta-LG-specific T cells in vivo. As a result, the decreased help to B cells by T cells would have reduced the antibody response to beta-LG. We conclude that suppression of the generation of T cell epitopes by conjugation with CMD is important to the mechanism for the reduced immunogenicity of beta-LG.

Adjuvants, Immunologic↗