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H H Fudenberg

Publications and source records attributed to H H Fudenberg.

At least 469 records · Page 26Linked to original sources
PubMed1970

Evidence for control of synthesis of the varible regions of the heavy chains of immunoglobulins G and M by the same gene.

Previous work indicated that the light chains of a monotypic immunoglobulins G2-K and M-K from a single patient (Ti1) are identical. Our present data show that the monotypic immunoglobulins G and M share idiotypic determinants not present in their isolated light chains or in any of a large number of other immunoglobulins tested, and that amino acid sequences of the first 27 residues from the NH(2)-terminal end of the gamma- and mu-chains are identical. These results support the hypothesis that at least two genes control the synthesis of each heavy and light chain and suggest that the monotypic immunoglobulin G and monotypic immunoglobulin M of this patient share three of the four genes involved. It is proposed that, during normal immunoglobulin synthesis, different cells of a single clone synthesize immunoglobulins M and G, and that the light chains and the variable segments of the heavy chains of the proteins of the two classes are identical within the clone. A genetic switching mechanism is suggested.

Amino Acid Sequence↗
PubMed1970

A variable region subclass of heavy chains common to immunoglobulins G, A, and M and characterized by an unblocked amino-terminal residue.

Heavy chains of IgG, IgA, and IgM classes of human immunoglobulins were compared by N-terminal residue determination and partial amino acid sequence analysis. A third subclass of the variable region of heavy chains was observed; an unblocked glutamic acid as the N-terminal residue is characteristic of this subclass. Our results indicated that the heavy chain variable region subclasses are not class specific, and that a given heavy chain variable region may be found in association with constant regions for mu-chains, alpha-chains, or gamma-chains of various subclasses.

Amino Acid Sequence↗
PubMed1970

Wiskott-Aldrich syndrome, a genetically determined cellular immunologic deficiency: clinical and laboratory responses to therapy with transfer factor.

Patients with diseases associated with defects in cellular immunity, such as the Wiskott-Aldrich syndrome, characteristically have severe recurrent infections and usually succumb to overwhelming infection at an early age. This communication describes a patient with this syndrome, defective delayed hypersensitivity by skin tests and by in vitro lymphocyte response, who was treated with dialysate of peripheral blood leukocytes (transfer factor). After treatment, the clinical status of the patient improved dramatically, concomitant with the development of delayed hypersensitivity to antigens to which the donor was sensitive. In vitro tests after transfer indicated that the patient's lymphocytes, when stimulated by specific antigen, produced migration inhibitory factor without concomitant DNA synthesis. These observations dissociate skin test sensitivity and activity of migration inhibitory factor from in vitro blastogenesis. Further, the response to phytohemagglutinin remained diminished before and after therapy. While these findings represent only an individual case, the climical results suggest that investigation of the use of transfer factor appears warranted in the therapy of Wiskott-Aldrich syndrome and other genetically-determined diseases associated with impaired cellular immunity.

Antigens↗
PubMed1970

The hyperviscosity syndrome. I. In IgG myeloma. The role of protein concentration and molecular shape.

The hyperviscosity syndrome is an uncommon complication in IgG myeloma. Its occurrence has been ascribed to the presence in the serum of high molecular weight polymers of the IgG proteins. Three patients with IgG myeloma and the clinical hyperviscosity syndrome were investigated, none of whom had IgG polymers in the serum by analytical ultracentrifugation. Relative serum viscosity in these patients ranged from 10 to 17.4 (normal 1.4-1.8). The total serum proteins ranged from 14 to 19 g/100 ml of which 10 to 17 g/100 ml was IgG globulin. Physicochemical studies of two of the isolated myeloma proteins indicated that they were of normal molecular weight (near 158,000 and 162,000). Protein Ca had a normal molecular radius (52.2 A) and configuration, (intrinsic viscosity of 5.5 cc/g, frictional ratio 1.48), but was present in very high concentration in the serum. Protein Pur had an increased molecular radius (58.2 A) and was asymmetrical (intrinsic viscosity 10.2 cc/g, frictional ratio 1.63). These results indicate that the concentration and molecular configuration of the myeloma protein are important determinants of the presence or absence of the hyperviscosity syndrome.

Blood Proteins↗