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Biomedical subjects

E C FRANKLIN

Publications and source records attributed to E C FRANKLIN.

At least 19 recordsLinked to original sources
PubMed1965

STRUCTURAL STUDIES OF HUMAN IMMUNOGLOBULINS. DIFFERENCES IN THE FD FRAGMENTS OF THE HEAVY CHAINS OF G MYELOMA PROTEINS.

1. Comparison of peptide maps of the Fc fragments of normal G immunoglobulins and 11 G myeloma proteins of the We (b) type showed them to be very similar except for differences associated with the Gm type. Some additional differences were noted, however, in the Fc fragments of three Vi (c) myeloma proteins. 2. Peptide maps of heavy chains from the same G myeloma proteins differed from each other and from normal heavy chains. In general, the myeloma chains contained a larger number of well defined spots; some of these were common to normal heavy chains while others were unique to each protein. Others, present in normal heavy chains, were lacking in the myeloma proteins. 3. Comparison of the heavy chains and Fc fragments from the same protein suggests that much of the variability of different myeloma proteins and, presumably, antibodies resides in the Fd fragment. 4. Further support for this is given by the finding that the antigenic specificity of 3 myeloma proteins also appeared to reside in the Fd fragments.

Antibodies↗
PubMed1964

STRUCTURAL STUDIES OF HUMAN 7S GAMMA-GLOBULIN (G IMMUNOGLOBULIN). FURTHER OBSERVATIONS OF A NATURALLY OCCURRING PROTEIN RELATED TO THE CRYSTALLIZABLE (FAST) FRAGMENT.

1. Detailed physical, chemical, and immunologic studies of a protein closely related to the Fc fragment and heavy chain of G immunoglobulin (IgG), and elaborated by a subject with a lymphoproliferative disorder are presented. 2. The protein, which has a molecular weight of 51,000, was cleaved into two half molecules by reduction and alkylation. 3. The protein has few if any of the antigenic determinants of the antigen-binding (Fab) papain fragment of IgG, and has a striking similarity in its antigenic properties to the Fc fragment. 4. Fingerprint patterns resemble those of the crystallizable (Fc) fragment, and lack several peptides found in the heavy chain. 5. These findings suggest that the Fc fragment may be a real structural unit of IgG, and raise the possibility of the existence of three different types of polypeptide chains in G immunoglobulin.

Amino Acids↗
PubMed1964

GAMMA GLOBULIN METABOLISM IN RABBITS DURING THE ANAMNESTIC RESPONSE.

1. Gamma globulin metabolism and distribution were studied employing rabbit gamma globulin (RGG)I(131) 24 times in 13 control rabbits. Similar studies were performed before and during the ananmestic response in 4 rabbits previously sensitized with a polyvalent pneumococcal vaccine. 2. During the ananmestic response, gamma-globulin levels increased from 1.0 to 6.0 gm/100 ml, and the gamma-globulin pool increased from 0.7 to 4.7 gm/kg. There was no change in the intravascular-extravascular partition of gamma globulin. 3. Gamma globulin degradation increased from 0.06 to 0.33 gm/kg/day during the 28 days of the immunization period while gamma globulin synthesis increased even further to average 0.47 gm/kg/day. Following the attainment of elevated gamma globulin levels the fractional rate of RGG-I(131) turnover increased from 8.0 to 12.5 per cent/day. 4. No differences were noted in the metabolism of homologous or autologous gamma globulin regardless of the allotypic specificities.

Animals↗
PubMed1963

NEW SERUM GROUP, GM(P).

The agglutination that occurs when rheumatoid arthritis serum Pond is added to erythrocytes sensitized with anti-D serum Moore is inhibited in the presence of some normal serums. The inhibitor, tentatively named Gm(p), is associated only with 7S gamma globulins and is apparently different from other previously defined serum groups. It is much more common in Caucasians than in Negroes, and probably is determined by a simple dominant gene.

Black People↗
PubMed1963

Properties of guinea pig 7S antibodies. I. Electrophoretic separation of two types of guinea pig 7S antibodies.

Guinea pigs hyperimmunized with single protein antigens or hapten conjugates emulsified in complete adjuvants produced two types of precipitating antibodies with different electrophoretic mobilities. "Slow" migrating antibody generally appeared earlier and "fast" migrating antibody later in the course of immunization. Animals initially immunized by the intraperitoneal route with hapten conjugates without adjuvants produced primarily fast migrating antibody. Purified guinea pig antibodies were also separable into slow and fast migrating components by electrophoresis in supporting media. Using suitable antisera prepared in rabbits hyperimmunized with guinea pig serum, it was demonstrated that slow and fast antibodies have both common and distinct antigenic determinants. Analytical ultracentrifugation disclosed that both antibodies have sedimentation coefficients of approximately 7S. These antibodies have been designated guinea pig 7Sgamma(1) and 7Sgamma(2).

Animals↗