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E A KABAT

Publications and source records attributed to E A KABAT.

At least 19 recordsLinked to original sources
PubMed1965

STUDIES ON HUMAN ANTIBODIES. 3. AMINO ACID COMPOSITION OF FOUR ANTIBODIES FROM ONE INDIVIDUAL.

Antilevan, antidextran, antiteichoic acid, anti-"A" and normal gammaG, all isolated from a single human, as well as pooled gammaG and gammaM, were analyzed for amino acid content. Differences ranging from 7 to 32 residues were found among these antibodies in glycine, valine, leucine, tyrosine, arginine, lysine, and threonine content. These conspicuous differences in amino acid composition were not correlated with the Gm type of these antibodies. Hydroxylysine was found in two of the four antibodies, antidextran and antiteichoic acid, and in gammaM- immunoglobulin. No hydroxylysine was found in gammaG- globulins. These findings probably account for discrepancies in the literature concerning the occurrence of this residue in antibody protein.

Alanine↗
PubMed1964

SEPARATION OF TEICHOIC ACID OF STAPHYLOCOCCUS AUREUS INTO TWO IMMUNOLOGICALLY DISTINCT SPECIFIC POLYSACCHARIDES WITH ALPHA- AND BETA-N-ACETYLGLUCOSAMINYL LINKAGES RESPECTIVELY. ANTIGENICITY OF THEICHOIC ACIDS IN MAN.

Human sera were found to contain antibodies precipitating with each of two samples of teichoic acid of Staphylococcus aureus prior to immunization; these antibodies were probably formed as a result of contact or infection with this microorganism. Injection of teichoic acid into two individuals resulted in a rise in circulating antibody to teichoic acid; a third subject probably had a primary response to alpha-teichoic acid. Quantitative precipitin and agar diffusion studies revealed the presence of two distinct antibodies in the sera and showed that each specimen of teichoic acid was a mixture of two polymers an alpha-linked N-acetylglucosaminyl-ribitol polymer and a beta-linked N-acetylglucosaminyl-ribitol polymer, termed alpha- and beta-teichoic acids respectively. The alpha-teichoic acid anti-alpha-teichoic acid system was inhibited best by alpha-linked glucosaminides and the beta-anti-beta-teichoic acid system was inhibited best by a beta-linked glucosaminide. The alpha- and (beta-teichoic acids could be separated from each other by specific precipitation under appropriate conditions and recovered from the washed specific precipitates. The existence of two distinct teichoic acid polymers raises important questions as to cell wall structure and the biosynthesis of the teichoic acids.

Bacteriological Techniques↗
PubMed1964

STUDIES ON HUMAN ANTIBODIES. I. STARCH GEL ELECTROPHORESIS OF THE DISSOCIATED POLYPEPTIDE CHAINS.

Specific precipitates and purified human antibodies were reduced and alkylated and subjected to starch gel electrophoresis in 8 M urea to dissociate and separate the L and H polypeptide chains. Dissociated antibodies to dextran, levan, teichoic acid, blood group A substance, and tetanus toxoid showed sharp bands corresponding to L polypeptide chains. The patterns differed for antibodies of different specificities. Some differences were also seen among antibodies of the same specificity from different individuals. Purified antidextran antibodies showed particularly simple patterns resembling those of purified human gamma myeloma proteins. In some cases only one L chain band was present.

Antibodies↗
PubMed1964

STUDIES ON HUMAN ANTIBODIES. II. DISTRIBUTION OF GENETIC FACTORS.

Human antibodies against dextran, teichoic acid, blood group A substance, levan, tetanus toxoid, and nuclei were isolated and analyzed for their content of Gm(a), Gm(b), and Inv(a) gamma-globulin genetic factors. The majority of these antibodies contained all the genetic factors determined in the donor's whole gamma-globulin, but in many antibodies at very different concentrations. In a few instances specific factors could not be detected despite their presence in the individual's whole gamma-globulin. Different antibodies isolated from the serum of the same individual showed different relative concentrations of genetic factors. The distribution of genetic factors seen in certain isolated human antibodies appeared to approach the selective occurrence of these factors in myeloma proteins.

ABO Blood-Group System↗
PubMed1964

SPECIFIC FRACTIONATION OF HUMAN ANTIDEXTRAN ANTIBODIES. II. ASSAY OF HUMAN ANTIDEXTRAN SERA AND SPECIFICALLY FRACTIONATED PURIFIED ANTIBODIES BY MICROCOMPLEMENT FIXATION AND COMPLEMENT FIXATION INHIBITION TECHNIQUES.

Human antidextran of one individual, absorbed specifically on sephadex, was fractionated into two populations of antibody molecules by successive elution with oligosaccharides of the isomaltose series of increasing size. The purified antibody fractions and some whole antidextran sera were found to fix complement with dextrans of molecular weight of 195,000 and above. It could be demonstrated by quantitative microcomplement fixation inhibition assays that the antibody eluted with isomaltotriose had a higher affinity for smaller oligosaccharides relative to isomaltohexaose, indicating a high content of antibody molecules with smaller combining sites, while with the second fraction, eluted with isomaltohexaose, the small haptens were very poor inhibitors and the larger oligosaccharides inhibited readily, presumably due to a higher proportion of molecules with larger combining site size. Assays of similarly prepared fractions, obtained from earlier bleedings of the same individual (1), with inhibition of complement fixation were in good agreement with those obtained by inhibition of precipitation. The two purified antidextran fractions were shown to differ with respect to their complement-fixing capacity. The fraction with molecules with smaller size-combining sites fixed only about half as much complement per unit antibody N as did the fraction containing largely molecules with larger combining sites suggesting that the strength of complement fixation is affected by the strength of the antigen-antibody interaction.

Antibodies↗
PubMed1963

THE ACTION OF ENZYMES FROM CLOSTRIDIUM TERTIUM ON THE I ANTIGENIC DETERMINANT OF HUMAN ERYTHROCYTES.

A method was described for the partial purification of beta galactosidase and beta glucosaminidase from Clostridium tertium culture supernatants. Treatment of erythrocytes with preparations containing both enzymes decreases their ability to react with anti-I cold agglutinins, and with Type XIV antipneumococcal horse serum. Erythrocytes of blood group A(1) are altered more rapidly and extensively than are group O cells. The enzymatic treatment of stroma results in a decrease in ability to absorb anti-I agglutinins and the release of galactose and N-acetylglucosamine as monosaccharides. The data suggest that these two sugars may be structural units of the erythrocyte I determinant, but no direct evidence is available.

Antibodies↗
PubMed1962

Specific fractionation of a population of antidextran molecules with combining sites of various sizes.

Two human antidextran sera were each fractionated into two populations of antibody by specific absorption of the antidextran on an insoluble dextran (sephadex), washing away non-specific protein, eluting the first fraction of antibody with isomaltose or isomaltotriose, and the second fraction with isomaltohexaose. The differences in behavior of the purified antibody fractions alone, or reconstituted in serum, in quantitative inhibition studies with the isomaltose series of oligosaccharides, or in quantitative precipitin studies with NRC dextrans of graded molecular weight, could be ascribed to differences in the sizes of their combining sites. It was shown that the antibody fractions eluted with isomaltose or isomaltotriose were made up largely of antibodies inhibited readily by the smaller oligosaccharides and therefore having a higher proportion of molecules with smaller-sized combining sites; whereas those fractions eluted with isomaltohexaose contained primarily antibodies readily inhibitable only with the larger oligosaccharides, and hence were considered to have a higher proportion of larger-sized combining sites. The purified antibody fractions were shown to be only fast gamma globulin,-to possess the same mobility in immunoelectrophoresis; in addition the antibody fractions from one individual in double diffusion in agar gave lines which fused with one another, with gamma globulin Fr. II, and with a purified antidextran solution containing the entire population of antidextran antibodies. Evidence was also presented which indicated little or no change in the populations of antibody molecules produced in these two individuals for a period as long as 10 years following immunization. It is felt that these data offer substantial support for the hypothesis that the antidextran produced in a single individual consists of a heterogeneous population of antibody molecules with antibody-combining sites of various sizes.

Antibodies↗